IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ. Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2003 Cordell SC., Robinson EJ., Lowe J. PDBe - Data obtained from the Protein Data Bank Europe in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Cordell SC., Robinson EJ., Lowe J. PDBe - Data obtained from the Protein Data Bank Europe Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2003 Biochemical analysis of alginate biosynthesis protein AlgX from Pseudomonas aeruginosa: purification of an AlgX-MucD (AlgY) protein complex. Biochemical analysis of alginate biosynthesis protein AlgX from Pseudomonas aeruginosa: purification of an AlgX-MucD (AlgY) protein complex. Biochimie (0300-9084) 2006 Gutsche J., Remminghorst U., Rehm BH. The cytoplasmic membrane with the non-ionic detergent Triton X-100. Figure 1. B.Rehm@massey.ac.nz ictbu Ictiobus bubalus (Smallmouth buffalo fish) Catostomus bubalus affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom ms participant Identification by mass spectrometry ms participant Gutsche J., Remminghorst U., Rehm BH. The cytoplasmic membrane with the non-ionic detergent Triton X-100. Figure 1. B.Rehm@massey.ac.nz Annotation to indicate that this entry has been checked and accepted by a senior curator. Biochimie (0300-9084) 2006 Bacterial two-hybrid analysis of interactions between region 4 of the sigma(70) subunit of RNA polymerase and the transcriptional regulators Rsd from Escherichia coli and AlgQ from Pseudomonas aeruginosa. Bacterial two-hybrid analysis of interactions between region 4 of the sigma(70) subunit of RNA polymerase and the transcriptional regulators Rsd from Escherichia coli and AlgQ from Pseudomonas aeruginosa. J. Bacteriol. (0021-9193) 2001 imex curation Dove SL., Hochschild A. Data from fig 2 and 4 could not be included since details of the origin of the DNA and regions of interaction were absent from the publication. The transcriptional complementation was studied with proteins fused to alpha RNAP (bait) and lambda CI (prey). ahochschild@hms.harvard.edu 09-April-2009: Contacted by JYOTI. davet Only protein-protein interactions ecoli Escherichia coli (strain K12) 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Dove SL., Hochschild A. Data from fig 2 and 4 could not be included since details of the origin of the DNA and regions of interaction were absent from the publication. The transcriptional complementation was studied with proteins fused to alpha RNAP (bait) and lambda CI (prey). ahochschild@hms.harvard.edu Accepted 2009-MAR-24 by DAVET. 09-April-2009: Contacted by JYOTI. J. Bacteriol. (0021-9193) 2001 davet Only protein-protein interactions imex curation Crystal structure and induction mechanism of AmiC-AmiR: a ligand-regulated transcription antitermination complex. Crystal structure and induction mechanism of AmiC-AmiR: a ligand-regulated transcription antitermination complex. EMBO J. (0261-4189) 1999 O'Hara BP., Norman RA., Wan PT., Roe SM., Barrett TE., Drew RE., Pearl LH. PDBe - Data obtained from the Protein Data Bank Europe in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined O'Hara BP., Norman RA., Wan PT., Roe SM., Barrett TE., Drew RE., Pearl LH. PDBe - Data obtained from the Protein Data Bank Europe EMBO J. (0261-4189) 1999 rpod_ecoli RNA polymerase sigma factor RpoD rpoD alt b3067 Sigma-70 JW3039 protein protein ecoli Escherichia coli (strain K12) MEQNPQSQLKLLVTRGKEQGYLTYAEVNDHLPEDIVDSDQIEDIIQMINDMGIQVMEEAPDADDLMLAENTADEDAAEAAAQVLSSVESEIGRTTDPVRMYMREMGTVELLTREGEIDIAKRIEDGINQVQCSVAEYPEAITYLLEQYDRVEAEEARLSDLITGFVDPNAEEDLAPTATHVGSELSQEDLDDDEDEDEEDGDDDSADDDNSIDPELAREKFAELRAQYVVTRDTIKAKGRSHATAQEEILKLSEVFKQFRLVPKQFDYLVNSMRVMMDRVRTQERLIMKLCVEQCKMPKKNFITLFTGNETSDTWFNAAIAMNKPWSEKLHDVSEEVHRALQKLQQIEEETGLTIEQVKDINRRMSIGEAKARRAKKEMVEANLRLVISIAKKYTNRGLQFLDLIQEGNIGLMKAVDKFEYRRGYKFSTYATWWIRQAITRSIADQARTIRIPVHMIETINKLNRISRQMLQEMGREPTPEELAERMLMPEDKIRKVLKIAKEPISMETPIGDDEDSHLGDFIEDTTLELPLDSATTESLRAATHDVLAGLTAREAKVLRMRFGIDMNTDYTLEEVGKQFDVTRERIRQIEAKALRKLRHPSRSEVLRSFLDD DIP protein P00579 original sequence version: 148 DIP protein P00579 original sequence version: 114 DIP protein P00579 original sequence version: 162 DIP protein P00579 original sequence version: 136 DIP protein P00579 original sequence version: null CA4F0E30DEC1703D rpod_pseae RNA polymerase sigma factor RpoD rpoD rpoDA Sigma-70 PA0576 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSGKAQQQSRLKELIARGREQGYLTYAEVNDHLPEDISDPEQVEDIIRMINDMGINVFETAPDADALLLAEADTDEAAAEEAAAALAAVESDIGRTTDPVRMYMREMGTVELLTREGEIEIAKRIEEGIREVMSAIAQFPGTVDSILADYNRIVAEGGRLSDVLSGYIDPDDGSLPAEEVEPVNLKDDSADSKEKDDEEEESDDSSDSDDEGDGGPDPEEARLRFTAVSEQLDKAKKALKKHGRGSKQATAELTGLAELFMPIKLVPKQFDALVARVRSALEGVRAQERAIMQLCVRDARMPRADFLRLFPNHETDEKWVDSVLKSKPKYAEAIERLRDDILRNQQKLAALESEVELTVAEIKEINRAMSIGEAKARRAKKEMVEANLRLVISIAKKYTNRGLQFLDLIQEGNIGLMKAVDKFEYRRGYKFSTYATWWIRQAITRSIADQARTIRIPVHMIETINKLNRISRQMLQEMGREPTPEELGERMDMPEDKIRKVLKIAKEPISMETPIGDDEDSHLGDFIEDSTMQSPIEMATSESLKESTREVLAGLTAREAKVLRMRFGIDMNTDHTLEEVGKQFDVTRERIRQIEAKALRKLRHPSRSEHLRSFLDE D82C2049DADCC24F amic_pseae Aliphatic amidase expression-regulating protein amiC PA3364 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MGSHQERPLIGLLFSETGVTADIERSQRYGALLAVEQLNREGGVGGRPIETLSQDPGGDPDRYRLCAEDFIRNRGVRFLVGCYMSHTRKAVMPVVERADALLCYPTPYEGFEYSPNIVYGGPAPNQNSAPLAAYLIRHYGERVVFIGSDYIYPRESNHVMRHLYRQHGGTVLEEIYIPLYPSDDDVQRAVERIYQARADVVFSTVVGTGTAELYRAIARRYGDGRRPPIASLTTSEAEVAKMESDVAEGQVVVAPYFSSIDTAASRAFVQACHGFFPENATITAWAEAAYWQTLLLGRAAQAAGSWRVEDVQRHLYDICIDAPQGPVRVERQNNHSRLSSRIAEIDARGVFQVRWQSPEPIRPDPYVVVHNLDDWSASMGGGALP 33924B6C36017B79 algx_pseae Alginate biosynthesis protein AlgX algX Probable alginate O-acetyltransferase AlgX PA3546 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MKTRTSRLFRLSALAAGLCLAQAALAADPGAAPSYQALPAGNLCPAAAYDSRYNTKYLGFFTHLVQAQDDWLFRTTYDLRTDFGTSAEGWRELRALRDELKRKGIELVVVYQPTRGLVNREKLSPAEKAGFDYELAKKNYLATIARFRQAGIWTPDFSPLFDEKEEHAYYFKGDHHWTPHGARRSAKIVAETLKQVPGFEEIPKKQFESKRVGLLSKLGTFHKAAAQLCGNSYATQYVDRFETEPVGASDSGDLFGDGGNPQIALVGTSNSGPAYNFAGFLEEFSGADILNNAVSGGGFDSSLLAYMTSEEFHKNPPKILIWEFATHYDMAQKSFYRQAMPLVDNGCSGRKTVLSRKVKLRQGRNEVLLNSAALPIRSGSYVADVTYSDPSVHELKNTIWYMNGRREQLKIEQSKAVDTGGRYVFQLRNDSDWADQQFLSLEIEAPEDMPQGLEVQASICQAAPAKASQSVAGR D31FBD293547069A rsd_ecoli Regulator of sigma D rsd b3995 JW3959 protein protein ecoli Escherichia coli (strain K12) MLNQLDNLTERVRGSNKLVDRWLHVRKHLLVAYYNLVGIKPGKESYMRLNEKALDDFCQSLVDYLSAGHFSIYERILHKLEGNGQLARAAKIWPQLEANTQQIMDYYDSSLETAIDHDNYLEFQQVLSDIGEALEARFVLEDKLILLVLDAARVKHPA BDB699DAC440A808 ftsz_pseae Cell division protein FtsZ ftsZ PA4407 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MFELVDNIAQTAVIKVIGVGGGGGNAVNHMAKNNVEGVEFICANTDAQALKNIAARTVLQLGPGVTKGLGAGANPEVGRQAALEDRERISEVLEGADMVFITTGMGGGTGTGAAPIIAEVAKEMGILTVAVVTRPFPFEGRKRMQIADEGIRALAESVDSLITIPNEKLLTILGKDASLLAAFAKADDVLAGAVRGISDIIKRPGMINVDFADVKTVMSEMGMAMMGTGCASGPNRAREATEAAIRNPLLEDVNLQGARGILVNITAGPDLSLGEYSDVGNIIEQFASEHATVKVGTVIDADMRDELHVTVVATGLGARLEKPVKVVDNTVQGSAAQAAAPAQREQQSVNYRDLDRPTVMRNQSHGSAATAAKLNPQDDLDYLDIPAFLRRQAD 16ABF06FAB82710F amir_pseae Aliphatic amidase regulator amiR PA3363 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSANSLLGSLRELQVLVLNPPGEVSDALVLQLIRIGCSVRQCWPPPESFDVPVDVVFTSIFQNRHHDEIAALLAAGTPRTTLVALVEYESPAVLSQIIELECHGVITQPLDAHRVLPVLVSARRISEEMAKLKQKTEQLQERIAGQARINQAKALLMQRHGWDEREAHQYLSREAMKRREPILKIAQELLGNEPSA 306A4F30E8E4C6C0 algq_pseae Transcriptional regulatory protein AlgQ algQ algR2 Alginate regulatory protein AlgR2 PA5255 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MLESCRNAQERWGGVHQLIDRWLHERQQLVQAFDALSGIQAPAPNAEELQHFCQLLLDYVSAGHFEVYEQLTAEGKAFGDQRGLELAKQIFPRLEAITESALNFNDRCDNGDCREGACLIAELKVLRQQLHERFELEDCLIEVLHNAHSQSGAEGSAVPV 9836DEFE99D24EC6 q51415_pseai algY protein protein pseai Pseudomonas aeruginosa MTSPFKVVAVSGGTYRPSRTLVLTQALIAELGQSLPIDSRVIELTDIAAPLGATLARNQAPAELQAVLDEIESADLLLVASPVYRGSYPGLLKHLFDLIDLNALIDTPVLLAATGNTSATRGPRPPVAPAVQLLPGDHPAHRGLRQRGRLRQLPDRQRAAEGAHPPRRRARRAAVRRTLRTVEDRLRCADERVLVPPDPRRWPLPRHQPGRAAGLAVLPEAGGTGGRQPWLSRRTDPHPTLLRRLLGGGLGLAPLTERLRFLVAIRPGIVSPTVSARMTATLDPVRWAPADQRGHRRRSRREPRRRHPFSATPSATRSPTSSSGLAARPAGRGGGLPRQAHPRGERQGALSAAATAVSAAVLRRFLGGRPRTGRRTGGRLPDLGRAVGGGGGENRRRAPASGSPWAYGEVRHPPACDRPRNRRRSLARRGQADRTHLRRNHRRRAAVLRPFRSGRPATHGRAARRPPRSPGDPAEPLGRGRPGARRRRHRAGRRSAAGGGAHRRIRRARHRQLHLLRLSAPGRGLPLRRTGLPAAVRTLRQPGRSWDDQPDRVVRRNDRQRRAAGSRRRLSSRAPEEKPPVNAKTRPEAQTPLQIVRRLAADFAENAAERDVAGGTPKAERDALRRSGLLSLIIPREYGGLGASWSETLQTVRELARVDSSIAHVYGFQHLMLATVRLFSRPEQ CBCCE638F5675D7A sula_pseae Cell division inhibitor SulA PA3008 sulA protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MQTSHSLPSAQLPLFQEAFWASNGAPLLDDVIDSPSSASIEEPAAFSELSLSGLPGHCLTLLAPILRELSEEQDARWLTLIAPPASLTHEWLRRAGLNRERILLLQAKDNAAALALSCEALRLGRSHTVVSWLEPLSRAARKQLSRAAQLGQAQSLNIRLG 86117EB72E03BC1F asia_bpt4 10 kDa anti-sigma factor 10 kDa RNA polymerase-associated protein asiA Audrey Stevens' inhibitor protein protein bpt4 Enterobacteria phage T4 Bacteriophage T4 MNKNIDTVREIITVASILIKFSREDIVENRANFIAFLNEIGVTHEGRKLNQNSFRKIVSELTQEDKKTLIDEFNEGFEGVYRYLEMYTNK DIP protein P32267 original sequence version: 75 1802A150946F2D22 algx-algy 2 13 unspecified role unspecified role prey prey 8 unspecified role unspecified role bait bait c terminal Strep-tag II tag tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range physical association physical association amic-amir-1 4 7 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) 11 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) direct interaction direct interaction octameric, multimeric working 81.400%, free 74.400% 2.25A ftsz-q9hzj8-1 1 10 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction tetrameric, multimeric working 78.4100%, free 74.4600% 2.1A rpod-rsd-1 3 9 unspecified role unspecified role prey prey lambda ci tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 6 unspecified role unspecified role bait bait alpha rnap tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P26480:p.Arg600His mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R H Wed May 02 17:46:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg600his' Tue Jun 30 20:17:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg600His' physical association physical association 5A Rsd can interact with region 4 of 70 from P. aeruginosa, and AlgQ can interact with region 4 of 70 from E. coli. rpod-algq 3 5 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain alpha tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P00579:p.Arg596His mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R H Wed May 02 19:37:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg596his' Tue Jun 30 15:57:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg596His' 12 unspecified role unspecified role prey prey lambda ci tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association 5B Rsd can interact with region 4 of 70 from P. aeruginosa, and AlgQ can interact with region 4 of 70 from E. coli. rpod-algq-1 3 12 unspecified role unspecified role prey prey lambda ci tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 6 unspecified role unspecified role bait bait P26480:p.Arg600His mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R H Wed May 02 17:50:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg600his' Tue Jun 30 18:28:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg600His' alpha rnap tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association 3 Rsd can interact with region 4 of 70 from P. aeruginosa, and AlgQ can interact with region 4 of 70 from E. coli. rpod-asia-1 3 15 unspecified role unspecified role prey prey lambda ci tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 6 unspecified role unspecified role bait bait alpha rnap tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P26480:p.Arg600His mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R H Wed May 02 16:44:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg600his' Tue Jun 30 18:05:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg600His' physical association physical association 6 Figure 6B shows that the λcI-AsiA chimera activated transcription from the modified test promoter in the presence of the α-ς70 chimera derived from ς70 of either E. coli or P. aeruginosa (similar findings with the α-ς70 chimera from E. coli have been obtained by S. Pande and D. mpidb The Microbial Protein Interaction Database Control of Pseudomonas aeruginosa AlgW protease cleavage of MucA by peptide signals and MucB. Control of Pseudomonas aeruginosa AlgW protease cleavage of MucA by peptide signals and MucB. Mol. Microbiol. (0950-382X) 2009 imex curation Cezairliyan B.O., Sauer R.T. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps tag fluorescence tag visualisation by fluorescence tag fluorescence Cezairliyan B.O., Sauer R.T. Accepted 2013-FEB-08 by ORCHARD Mol. Microbiol. (0950-382X) 2009 Only protein-protein interactions imex curation Functional dissection of N-acetylglutamate synthase (ArgA) of Pseudomonas aeruginosa and restoration of its ancestral N-acetylglutamate kinase activity. Functional dissection of N-acetylglutamate synthase (ArgA) of Pseudomonas aeruginosa and restoration of its ancestral N-acetylglutamate kinase activity. J. Bacteriol. (0021-9193) 2012 imex curation Sancho-Vaello E., Fernandez-Murga M.L., Rubio V. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Sancho-Vaello E., Fernandez-Murga M.L., Rubio V. Accepted 2012-DEC-05 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2012 Only protein-protein interactions imex curation Interaction of penicillin-binding protein 2 with soluble lytic transglycosylase B1 in Pseudomonas aeruginosa. Interaction of penicillin-binding protein 2 with soluble lytic transglycosylase B1 in Pseudomonas aeruginosa. J. Bacteriol. (0021-9193) 2008 imex curation Legaree B.A., Clarke A.J. 04-Feb-2013: Contacted by IntAct-Help. Only protein-protein interactions pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom anti tag western anti tag western blot anti tag western Legaree B.A., Clarke A.J. Accepted 2013-JAN-28 by ORCHARD 04-Feb-2013: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2008 Only protein-protein interactions imex curation Control of Pseudomonas aeruginosa AlgW protease cleavage of MucA by peptide signals and MucB. Control of Pseudomonas aeruginosa AlgW protease cleavage of MucA by peptide signals and MucB. Mol. Microbiol. (0950-382X) 2009 imex curation Cezairliyan B.O., Sauer R.T. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Cezairliyan B.O., Sauer R.T. Accepted 2013-FEB-08 by ORCHARD Mol. Microbiol. (0950-382X) 2009 Only protein-protein interactions imex curation The CgrA and CgrC proteins form a complex that positively regulates cupA fimbrial gene expression in Pseudomonas aeruginosa. The CgrA and CgrC proteins form a complex that positively regulates cupA fimbrial gene expression in Pseudomonas aeruginosa. J. Bacteriol. (0021-9193) 2011 imex curation McManus H.R., Dove S.L. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) tap tandem affinity purification TAP TAP tap western blot western blot Immuno blot Immuno blot McManus H.R., Dove S.L. Accepted 2012-DEC-06 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2011 Only protein-protein interactions imex curation SagS contributes to the motile-sessile switch and acts in concert with BfiSR to enable Pseudomonas aeruginosa biofilm formation. SagS contributes to the motile-sessile switch and acts in concert with BfiSR to enable Pseudomonas aeruginosa biofilm formation. J. Bacteriol. (0021-9193) 2011 imex curation Petrova O.E., Sauer K. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) pull down pull down predetermined predetermined participant predetermined Petrova O.E., Sauer K. Accepted 2012-DEC-06 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2011 Only protein-protein interactions imex curation Interactions of the components of the general secretion pathway: role of Pseudomonas aeruginosa type IV pilin subunits in complex formation and extracellular protein secretion. Interactions of the components of the general secretion pathway: role of Pseudomonas aeruginosa type IV pilin subunits in complex formation and extracellular protein secretion. Mol. Microbiol. (0950-382X) 1997 imex curation Lu H.M., Motley S.T., Lory S. Actual strain used = PAK BS3 cross-linking 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink western blot western blot Immuno blot Immuno blot Lu H.M., Motley S.T., Lory S. Actual strain used = PAK BS3 cross-linking Accepted 2012-DEC-05 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. Mol. Microbiol. (0950-382X) 1997 Only protein-protein interactions imex curation Rsd family proteins make simultaneous interactions with regions 2 and 4 of the primary sigma factor. Rsd family proteins make simultaneous interactions with regions 2 and 4 of the primary sigma factor. Mol. Microbiol. (0950-382X) 2008 imex curation Yuan A.H., Gregory B.D., Sharp J.S., McCleary K.D., Dove S.L., Hochschild A. 04-Feb-2013: Contacted by IntAct-Help. Only protein-protein interactions ecoli Escherichia coli (strain K12) 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Yuan A.H., Gregory B.D., Sharp J.S., McCleary K.D., Dove S.L., Hochschild A. Accepted 2013-JAN-30 by ORCHARD 04-Feb-2013: Contacted by IntAct-Help. Mol. Microbiol. (0950-382X) 2008 Only protein-protein interactions imex curation Interaction of penicillin-binding protein 2 with soluble lytic transglycosylase B1 in Pseudomonas aeruginosa. Interaction of penicillin-binding protein 2 with soluble lytic transglycosylase B1 in Pseudomonas aeruginosa. J. Bacteriol. (0021-9193) 2008 imex curation Legaree B.A., Clarke A.J. 04-Feb-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Legaree B.A., Clarke A.J. Accepted 2013-JAN-28 by ORCHARD 04-Feb-2013: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2008 Only protein-protein interactions imex curation Fitting periplasmic membrane fusion proteins to inner membrane transporters: mutations that enable Escherichia coli AcrA to function with Pseudomonas aeruginosa MexB. Fitting periplasmic membrane fusion proteins to inner membrane transporters: mutations that enable Escherichia coli AcrA to function with Pseudomonas aeruginosa MexB. J. Bacteriol. (0021-9193) 2008 imex curation Krishnamoorthy G., Tikhonova E.B., Zgurskaya H.I. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions ecoli Escherichia coli (strain K12) crosslink cross-linking study crosslink predetermined predetermined participant predetermined Krishnamoorthy G., Tikhonova E.B., Zgurskaya H.I. Accepted 2012-DEC-05 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2008 Only protein-protein interactions imex curation ExsD inhibits expression of the Pseudomonas aeruginosa type III secretion system by disrupting ExsA self-association and DNA binding activity. ExsD inhibits expression of the Pseudomonas aeruginosa type III secretion system by disrupting ExsA self-association and DNA binding activity. J. Bacteriol. (0021-9193) 2010 imex curation Brutinel E.D., Vakulskas C.A., Yahr T.L. Only protein-protein interactions ecolx Escherichia coli gallex lex-a dimerization assay gallex predetermined predetermined participant predetermined Brutinel E.D., Vakulskas C.A., Yahr T.L. Accepted 2013-FEB-16 by ORCHARD J. Bacteriol. (0021-9193) 2010 Only protein-protein interactions imex curation Binding and spreading of ParB on DNA determine its biological function in Pseudomonas aeruginosa. Binding and spreading of ParB on DNA determine its biological function in Pseudomonas aeruginosa. J. Bacteriol. (0021-9193) 2011 imex curation Kusiak M., Gapczynska A., Plochocka D., Thomas C.M., Jagura-Burdzy G. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions ecolx Escherichia coli cosedimentation cosedimentation predetermined predetermined participant predetermined Kusiak M., Gapczynska A., Plochocka D., Thomas C.M., Jagura-Burdzy G. Accepted 2012-DEC-10 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2011 Only protein-protein interactions imex curation Functional Divergence of FimX in PilZ Binding and Type IV Pilus Regulation. Functional Divergence of FimX in PilZ Binding and Type IV Pilus Regulation. J. Bacteriol. (0021-9193) 2012 imex curation Qi Y., Xu L., Dong X., Yau Y.H., Ho C.L., Koh S.L., Shochat S.G., Chou S.H., Tang K., Liang Z.X. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Qi Y., Xu L., Dong X., Yau Y.H., Ho C.L., Koh S.L., Shochat S.G., Chou S.H., Tang K., Liang Z.X. Accepted 2012-DEC-05 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2012 Only protein-protein interactions imex curation Crystal structure of the Pseudomonas aeruginosa virulence factor regulator. Crystal structure of the Pseudomonas aeruginosa virulence factor regulator. J. Bacteriol. (0021-9193) 2011 imex curation Cordes T.J., Worzalla G.A., Ginster A.M., Forest K.T. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Cordes T.J., Worzalla G.A., Ginster A.M., Forest K.T. Accepted 2012-DEC-10 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2011 Only protein-protein interactions imex curation Protein modulator of multidrug efflux gene expression in Pseudomonas aeruginosa. Protein modulator of multidrug efflux gene expression in Pseudomonas aeruginosa. J. Bacteriol. (0021-9193) 2007 imex curation Daigle DM, Cao L, Fraud S, Wilke MS, Pacey A, Klinoski R, Strynadka NC, Dean CR, Poole K poolek@post.queensu.ca 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions ecolx Escherichia coli gallex lex-a dimerization assay gallex predetermined predetermined participant predetermined Daigle DM, Cao L, Fraud S, Wilke MS, Pacey A, Klinoski R, Strynadka NC, Dean CR, Poole K poolek@post.queensu.ca. poolek@post.queensu.ca Accepted 2012-DEC-14 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2007 Only protein-protein interactions imex curation TagR promotes PpkA-catalysed type VI secretion activation in Pseudomonas aeruginosa. TagR promotes PpkA-catalysed type VI secretion activation in Pseudomonas aeruginosa. Mol. Microbiol. (0950-382X) 2009 imex curation Hsu F., Schwarz S., Mougous J.D. Only protein-protein interactions pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) tap tandem affinity purification TAP TAP tap western blot western blot Immuno blot Immuno blot Hsu F., Schwarz S., Mougous J.D. Accepted 2013-FEB-11 by ORCHARD Mol. Microbiol. (0950-382X) 2009 Only protein-protein interactions imex curation The CgrA and CgrC proteins form a complex that positively regulates cupA fimbrial gene expression in Pseudomonas aeruginosa. The CgrA and CgrC proteins form a complex that positively regulates cupA fimbrial gene expression in Pseudomonas aeruginosa. J. Bacteriol. (0021-9193) 2011 imex curation McManus H.R., Dove S.L. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions ecolx Escherichia coli 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined McManus H.R., Dove S.L. Accepted 2012-DEC-06 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2011 Only protein-protein interactions imex curation PAS Domain Residues and Prosthetic Group Involved in BdlA-Dependent Dispersion Response by Pseudomonas aeruginosa Biofilms. PAS Domain Residues and Prosthetic Group Involved in BdlA-Dependent Dispersion Response by Pseudomonas aeruginosa Biofilms. J. Bacteriol. (0021-9193) 2012 imex curation Petrova O.E., Sauer K. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) pull down pull down anti tag western anti tag western blot anti tag western Petrova O.E., Sauer K. Accepted 2012-DEC-05 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2012 Only protein-protein interactions imex curation Protein modulator of multidrug efflux gene expression in Pseudomonas aeruginosa. Protein modulator of multidrug efflux gene expression in Pseudomonas aeruginosa. J. Bacteriol. (0021-9193) 2007 imex curation Daigle DM, Cao L, Fraud S, Wilke MS, Pacey A, Klinoski R, Strynadka NC, Dean CR, Poole K poolek@post.queensu.ca 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Daigle DM, Cao L, Fraud S, Wilke MS, Pacey A, Klinoski R, Strynadka NC, Dean CR, Poole K poolek@post.queensu.ca. poolek@post.queensu.ca Accepted 2012-DEC-14 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2007 Only protein-protein interactions imex curation Assembly of the MexAB-OprM multidrug pump of Pseudomonas aeruginosa: component interactions defined by the study of pump mutant suppressors. Assembly of the MexAB-OprM multidrug pump of Pseudomonas aeruginosa: component interactions defined by the study of pump mutant suppressors. J. Bacteriol. (ISSN:0021-9193) 2007 imex curation Nehme D, Poole K 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) pull down pull down western blot western blot Immuno blot Immuno blot Nehme D, Poole K Accepted 2012-DEC-14 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (ISSN:0021-9193) 2007 Only protein-protein interactions imex curation Cochaperone interactions in export of the type III needle component PscF of Pseudomonas aeruginosa. Cochaperone interactions in export of the type III needle component PscF of Pseudomonas aeruginosa. J. Bacteriol. (0021-9193) 2010 imex curation Ple S., Job V., Dessen A., Attree I. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions ecolx Escherichia coli pull down pull down western blot western blot Immuno blot Immuno blot Ple S., Job V., Dessen A., Attree I. Accepted 2012-DEC-05 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2010 Only protein-protein interactions imex curation Use of cell wall stress to characterize sigma 22 (AlgT/U) activation by regulated proteolysis and its regulon in Pseudomonas aeruginosa. Use of cell wall stress to characterize sigma 22 (AlgT/U) activation by regulated proteolysis and its regulon in Pseudomonas aeruginosa. Mol. Microbiol. (0950-382X) 2009 imex curation Wood L.F., Ohman D.E. 04-Feb-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Wood L.F., Ohman D.E. Accepted 2013-JAN-18 by ORCHARD 04-Feb-2013: Contacted by IntAct-Help. Mol. Microbiol. (0950-382X) 2009 Only protein-protein interactions imex curation Bacteria possessing two RelA/SpoT-like proteins have evolved a specific stringent response involving the acyl carrier protein-SpoT interaction. Bacteria possessing two RelA/SpoT-like proteins have evolved a specific stringent response involving the acyl carrier protein-SpoT interaction. J. Bacteriol. (0021-9193) 2009 imex curation Battesti A., Bouveret E. Only protein-protein interactions ecolx Escherichia coli adenylate cyclase adenylate cyclase complementation bacterial two-hybrid bacterial two-hybrid adenylate cyclase predetermined predetermined participant predetermined Battesti A., Bouveret E. Accepted 2013-JAN-31 by ORCHARD J. Bacteriol. (0021-9193) 2009 Only protein-protein interactions imex curation Acyl-homoserine lactone binding to and stability of the orphan Pseudomonas aeruginosa quorum-sensing signal receptor QscR. Acyl-homoserine lactone binding to and stability of the orphan Pseudomonas aeruginosa quorum-sensing signal receptor QscR. J. Bacteriol. (0021-9193) 2011 imex curation Oinuma K., Greenberg E.P. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Oinuma K., Greenberg E.P. Accepted 2012-DEC-12 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2011 Only protein-protein interactions imex curation ExsD inhibits expression of the Pseudomonas aeruginosa type III secretion system by disrupting ExsA self-association and DNA binding activity. ExsD inhibits expression of the Pseudomonas aeruginosa type III secretion system by disrupting ExsA self-association and DNA binding activity. J. Bacteriol. (0021-9193) 2010 imex curation Brutinel E.D., Vakulskas C.A., Yahr T.L. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Brutinel E.D., Vakulskas C.A., Yahr T.L. Accepted 2013-FEB-16 by ORCHARD J. Bacteriol. (0021-9193) 2010 Only protein-protein interactions imex curation Control of Pseudomonas aeruginosa AlgW protease cleavage of MucA by peptide signals and MucB. Control of Pseudomonas aeruginosa AlgW protease cleavage of MucA by peptide signals and MucB. Mol. Microbiol. (0950-382X) 2009 imex curation Cezairliyan B.O., Sauer R.T. Only protein-protein interactions in vitro In vitro protease assay protease assay weight by comassie molecular weight estimation by coomasie staining weight by comassie Cezairliyan B.O., Sauer R.T. Accepted 2013-FEB-08 by ORCHARD Mol. Microbiol. (0950-382X) 2009 Only protein-protein interactions imex curation Binding and spreading of ParB on DNA determine its biological function in Pseudomonas aeruginosa. Binding and spreading of ParB on DNA determine its biological function in Pseudomonas aeruginosa. J. Bacteriol. (0021-9193) 2011 imex curation Kusiak M., Gapczynska A., Plochocka D., Thomas C.M., Jagura-Burdzy G. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions ecolx Escherichia coli crosslink cross-linking study crosslink predetermined predetermined participant predetermined Kusiak M., Gapczynska A., Plochocka D., Thomas C.M., Jagura-Burdzy G. Accepted 2012-DEC-10 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2011 Only protein-protein interactions imex curation q9i751_pseae fha1 PA0081 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MPLRLTITSYHKLTPGQCSEKVLDQGQLTIGRGPDNDWVLPDPERLVSSRHCTILNRDGVYYLTDTSTNGVLLVNAGHRLRRGNSEPLQDGETVRLGEYDILVQLGHDIALPGSGNPQTDPFTSFDALMSRQAAGSAPAFAEPAPTPHPAVTAHFQGGSPLDTKPDLFDFLTPPPPGAAPRPDHVPAEQHDFRPPEPVIPPPPATTPAPPPAGGAPLIPADWDPFAELLGNTPAPSATPVAQPLPTAEPTPLAMPFADPGITQQPQPQPQPQPQPQPQPQPQPQPASVAAPTPPASAAASAGGDLLQAFLRGAGMTQLKVDPAGAEAQMEAIGRSYRGLVEGLVDVLRARASLKGEFRMAQTMIQPVQNNPLKFAPNVDEAMLLLLRRDNQAFMAPDRAVADSFEDLKAHQLAVMAGVQAAIRHLLARFEPAALEARFGKPAGLSGLLPGARQAQNWDSFTELYAKILREAEDDFQELFGREFSRAYEEHSARLRRS A6C63E1D287E7272 q9hwi5_pseae PA4196 bfiR protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MAMPDEALVYVVDDDQGMLESTVWLLESVGLKARPFTQGRDFLDACEGGRHACVLLDVRMPGMGGLNVQDELLARGIDLPVIFVSGHADVPIVVRAFKAGAVDFIEKPYNEQLLLDSVQQALDRHARRRRHHDLDAGLHERLDSLTPRERDVLLPLVRGYTSREVAEQLEVSVKTVDLYRARVMKRMQAQTLPELVGMAIAAGLVDPLRLREGT 5BCAA7998A352799 arga_pseae Amino-acid acetyltransferase argA N-acetylglutamate synthase PA5204 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MPDYVNWLRHASPYINSHRDRTFVVMLPGEGVEHPNFGNIVHDLVLLHSLGARLVLVHGSRPQIEARLAARGLAPRYHRDLRVTDAPTLECVIDAVGSLRIAIEARLSMDMAASPMQGARLRVAGGNLVTARPIGVVEGVDYHHTGEVRRIDRKGIGRLLDERSIVLLSPLGYSPTGEIFNLACEDVAMRAAIDLEAEKLILYGAEQGLLDASGKLVRELRPQQVPAHLQRLGNSYQAELLDAAAQACRAGVKRSHIVSYTEDGALLSELFTRTGNGTLVAQEQFEQLREAGIEDVGGLIELIRPLEEQGILVRRSREVLEREIEQFSIVEREGLIIACAALYPIADSEAGELACLAVNPEYRHGGRGDELLERIEERARGLGLKTLFVLTTRTAHWFRERGFQPSSVERLPAARASLYNFQRNSQVFEKSL 725FAD778FD44A4E psce_pseae Type III export protein PscE Pseudomonas secretion protein E PA1718 pscE protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MMTALETRLSVADGTHAAALRQRLQAALAECRRELARGACPEHFQFLQQQARALEGGLGILSQLTED DIP protein Q9I317 original sequence version: 66 62339AFECA931617 q9hxs2_pseae armR PA3719 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSLNTPRNKPSRTETEAVAASSGRSAVGRRDYTEQLRRAARRNAWDLYGEHFY DF2B22DB8CD1287B q9i524_pseae relA PA0934 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MVQVRAHQPVNTDGSINLEAWLDHVQNLVPGLDRQGLLEACEFARESEQRAIAAQNSWAEGTSSFQTGLEIAEILADLKLDQESLVAAVIYRGVREGKITLEAVNKHFGPVVAKLIEGVLRMAAISASLNPRHSMVLGTQAQVENLRKMLVAMVDDVRVALIKLAERTCAIRAVKNADEEKRHRVAREVFDIYAPLAHRLGIGHIKWELEDLSFRYLEPDQYKQIAKLLHERRLDREQYIANVMSQLKEALAATGVQADLSGRAKHIYSIWRKMQRKGLDFSQIYDVRAVRVLVPEMRDCYTALGIVHTLWRHIPKEFDDYIANPKENGYRSLHTAVIGPEGKVLEVQIRTHSMHEEAELGVCAHWRYKGTDVKASSNHYEEKISWLRQVLEWHEELGDIGGLAEQLRVDIEPDRVYVFTPDGHAIDLPKGATPLDFAYRVHTEVGHNCRGAKINGRIVPLNYSLQTGEQVEIITGKHSGPSRDWLNSNLGYVTTSRARAKIVHWFKLQARDQNVAAGKALIERELSRLALPPVDFDRLAEKANVRTAEDMFAALGAGDLRLAHLVNYAQQLVEPDRDSEQLELIPRKPSKIGHGKRGDVQIQGVGNLLTQMAGCCQPLPGDPIVGYITLGRGVTIHRQDCATALQLAGREPERMIQVSWGPEPVRTYPVDIAIRAYDRSGLLRDVSQVLLNERINVLAVNTRSNKEDNTATMQLTIEIPGLDALGRLLARVSQLPNIIEARRNRTP 0D0729D311E6D82D mucb_pseae Sigma factor AlgU regulatory protein MucB mucB algN PA0764 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MRTTSLLLLLGSLMAVPATQAADASDWLNRLAEADRQNSFQGTFVYERNGSFSTHEIWHRVESDGAVRERLLQLDGARQEVVRVDGRTQCISGGLADQLADAQLWPVRKFDPSQLASWYDLRLVGESRVAGRPAVVLAVTPRDQHRYGFELHLDRDTGLPLKSLLLNEKGQLLERFQFTQLNTGAAPAEDQLQAGAECQVVGPAKADGEKTVAWRSEWLPPGFTLTRSFMRRSPVTPDPVACLTYGDGLARFSVFIEPLHGAMVGDARSQLGPTVVVSKRLQTDDGGQMVTVVGEVPLGTAERVALSIRPEAAAQK DC13C21A7BBB9C2C algq_pseae Transcriptional regulatory protein AlgQ algQ algR2 Alginate regulatory protein AlgR2 PA5255 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MLESCRNAQERWGGVHQLIDRWLHERQQLVQAFDALSGIQAPAPNAEELQHFCQLLLDYVSAGHFEVYEQLTAEGKAFGDQRGLELAKQIFPRLEAITESALNFNDRCDNGDCREGACLIAELKVLRQQLHERFELEDCLIEVLHNAHSQSGAEGSAVPV 9836DEFE99D24EC6 mexr_pseae Multidrug resistance operon repressor mexR PA0424 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MNYPVNPDLMPALMAVFQHVRTRIQSELDCQRLDLTPPDVHVLKLIDEQRGLNLQDLGRQMCRDKALITRKIRELEGRNLVRRERNPSDQRSFQLFLTDEGLAIHQHAEAIMSRVHDELFAPLTPVEQATLVHLLDQCLAAQPLEDI 59F5146394BE89DD 59F5146394BE89DD q9hvx1_pseae Probable periplasmic serine endoprotease DegP-like algW Protease Do PA4446 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MPKALRFLGWPVLVGVLLALLIIQHNPELVGLPRQEVHVEQAPLLSRLQEGPVSYANAVSRAAPAVANLYTTKMVSKPSHPLFDDPMFRRFFGDNLPQQKRMESSLGSAVIMSAEGYLLTNNHVTAGADQIIVALRDGRETIAQLVGSDPETDLAVLKIDLKNLPAMTLGRSDGIRTGDVCLAIGNPFGVGQTVTMGIISATGRNQLGLNTYEDFIQTDAAINPGNSGGALVDAAGNLIGINTAIFSKSGGSQGIGFAIPTKLALEVMQSIIEHGQVIRGWLGVEVKALTPELAESLGLGETAGIVVAGVYRDGPAARGGLLPGDVILTIDKQEASDGRRSMNQVARTRPGQKISIVVLRNGQKVNLTAEVGLRPPPAPAPQQKQDGGE BC3ED49CC6EFE75F clpv1_pseae AAA+ ATPase ClpV1 PA0090 clpV1 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSEISRVALFGKLNSLAYKAIEAATVFCKLRGNPYVELVHWFHQILQLPDSDLHQIVRQSGIDPARLAKDLTEALDRLPRGSTSITDLSSHVEEAVERGWVYGSLMFGESQVRTGYLVIGILKTPSLRHALTGLSAEFAKLKVEALTERFDEYVGASPENGLSASDGFNAGAAPGEASGALAPSAMGKQEALKRFTVDLTEQARSGKLDPIVGRDEEIRQLVDILMRRRQNNPILTGEAGVGKTAVVEGFALRIVAGDVPPALKDVELRALDVGLLQAGASMKGEFEQRLRQVIEDVQSSEKPIILFIDEAHTLVGAGGAAGTGDAANLLKPALARGTLRTVAATTWAEYKKHIEKDPALTRRFQVVQVDEPSEHKAILMMRGVASTMEKHHQVQILDEALEAAVRLSHRYIPARQLPDKSVSLLDTACARTAISLHAVPAEVDDSRRRIEALETELAIIRRESAIGVATAERQRNAETLLAEERERLAALEQRWAEEKRLVDELLETRARLRAAAEAVDAGGVPLGEGEVRLDEEQRQALHARLAELQAQLSALQGEEPLILPTVDYQAVASVVADWTGIPVGRMARNEIETVLNLDRHLKKRIIGQDHALEMIAKRIQTSRAGLDNPSKPIGVFMLAGTSGVGKTETALALAEAMYGGEQNVITINMSEFQEAHTVSTLKGAPPGYIGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVHEIFFQVFDKGVMEDGEGRVIDFKNTLILLTTNAGTEMIASLCADPELMPEPEAIAKSLREPLLKIFPPALLGRLVTIPYYPLSDDMLKAISRLQLGRIKKRVEATHKVPFEFDEGVVDLIVSRCTETESGGRMIDAILTNTLLPDMSREFLTRMLEGKPLAGVRISSRDNQFHYDFAEAE DB45A33B091C0071 g3xd77_pseae qscR PA1898 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MHDEREGYLEILSRITTEEEFFSLVLEICGNYGFEFFSFGARAPFPLTAPKYHFLSNYPGEWKSRYISEDYTSIDPIVRHGLLEYTPLIWNGEDFQENRFFWEEALHHGIRHGWSIPVRGKYGLISMLSLVRSSESIAATEILEKESFLLWITSMLQATFGDLLAPRIVPESNVRLTARETEMLKWTAVGKTYGEIGLILSIDQRTVKFHIVNAMRKLNSSNKAEATMKAYAIGLLN D4A62CD5ADDD57EE q9ht12_pseae Probable chromosome-partitioning protein ParB spoOJ PA5562 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MAAKKRGLGRGLDALLGGSSPAKLQEEAVQADRRELQQIPLDLMQRGKYQPRRDMDPQALEELAQSIKAQGVMQPIVVRPIANGRYEIIAGERRWRASQQAGLEKIPALVRDVPDEAAIAMALIENIQREDLNPIEEAAALQRLQQEFQLTQQQVAEAVGKSRATITNLLRLIGLPEEIKTLLSHGDLEMGHARALLGLPAERQVEGARHVVAHGLTVRQTEALVRQWTHAPGKPAGPVKSDPDIARLEQRLAERLGASVQIRHGQKGKGQLVIRYSSLDELQGVLAHIR CCD3A21204B12C37 gspg_pseae Type II secretion system core protein G xcpT pddA PA3101 General secretion pathway protein G PilD-dependent protein PddA protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MQRRQQSGFTLIEIMVVVVILGILAALVVPQVMSRPDQAKVTVAKGDIKAIAAALDMYKLDNFAYPSTQQGLEALVKKPTGNPQPKNWNKDGYLKKLPVDPWGNPYQYLAPGTKGPFDLYSLGADGKEGGSDNDADIGNWDN B498621CFC45B9B7 exsc_pseae Transcriptional anti-antiactivator ExsC exsC PA1710 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MDLTSKVNRLLAEFAGRIGLPSLSLDEEGMASLLFDEQVGVTLLLLAERERLLLEADVAGIDVLGEGIFRQLASFNRHWHRFDLHFGFDELTGKVQLYAQILAAQLTLECFEATLANLLDHAEFWQRLLPCDSDREAVAAVGMRV A53BEB27270EA737 rpod_pseae RNA polymerase sigma factor RpoD rpoD rpoDA Sigma-70 PA0576 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSGKAQQQSRLKELIARGREQGYLTYAEVNDHLPEDISDPEQVEDIIRMINDMGINVFETAPDADALLLAEADTDEAAAEEAAAALAAVESDIGRTTDPVRMYMREMGTVELLTREGEIEIAKRIEEGIREVMSAIAQFPGTVDSILADYNRIVAEGGRLSDVLSGYIDPDDGSLPAEEVEPVNLKDDSADSKEKDDEEEESDDSSDSDDEGDGGPDPEEARLRFTAVSEQLDKAKKALKKHGRGSKQATAELTGLAELFMPIKLVPKQFDALVARVRSALEGVRAQERAIMQLCVRDARMPRADFLRLFPNHETDEKWVDSVLKSKPKYAEAIERLRDDILRNQQKLAALESEVELTVAEIKEINRAMSIGEAKARRAKKEMVEANLRLVISIAKKYTNRGLQFLDLIQEGNIGLMKAVDKFEYRRGYKFSTYATWWIRQAITRSIADQARTIRIPVHMIETINKLNRISRQMLQEMGREPTPEELGERMDMPEDKIRKVLKIAKEPISMETPIGDDEDSHLGDFIEDSTMQSPIEMATSESLKESTREVLAGLTAREAKVLRMRFGIDMNTDHTLEEVGKQFDVTRERIRQIEAKALRKLRHPSRSEHLRSFLDE D82C2049DADCC24F arca_ecoli Aerobic respiration control protein ArcA Dye resistance protein arcA cpxC dye fexA msp seg sfrA b4401 JW4364 protein protein ecoli Escherichia coli (strain K12) MQTPHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSEYDINLVIMDINLPGKNGLLLARELREQANVALMFLTGRDNEVDKILGLEIGADDYITKPFNPRELTIRARNLLSRTMNLGTVSEERRSVESYKFNGWELDINSRSLIGPDGEQYKLPRSEFRAMLHFCENPGKIQSRAELLKKMTGRELKPHDRTVDVTIRRIRKHFESTPDTPEIIATIHGEGYRFCGDLED 9316CF4DE8EABDE8 tolc_ecoli Outer membrane protein TolC tolC mtcB mukA refI Multidrug efflux pump subunit TolC Outer membrane factor TolC colE1-i toc weeA JW5503 b3035 protein protein ecoli Escherichia coli (strain K12) MKKLLPILIGLSLSGFSSLSQAENLMQVYQQARLSNPELRKSAADRDAAFEKINEARSPLLPQLGLGADYTYSNGYRDANGINSNATSASLQLTQSIFDMSKWRALTLQEKAAGIQDVTYQTDQQTLILNTATAYFNVLNAIDVLSYTQAQKEAIYRQLDQTTQRFNVGLVAITDVQNARAQYDTVLANEVTARNNLDNAVEQLRQITGNYYPELAALNVENFKTDKPQPVNALLKEAEKRNLSLLQARLSQDLAREQIRQAQDGHLPTLDLTASTGISDTSYSGSKTRGAAGTQYDDSNMGQNKVGLSFSLPIYQGGMVNSQVKQAQYNFVGASEQLESAHRSVVQTVRSSFNNINASISSINAYKQAVVSAQSSLDAMEAGYSVGTRTIVDVLDATTTLYNAKQELANARYNYLINQLNIKSALGTLNEQDLLALNNALSKPVSTNPENVAPQTPEQNAIADGYAPDSPAPVVQQTSARTTTSNGHNPFRN DIP protein P02930 original sequence version: 151 DIP protein P02930 original sequence version: 112 DIP protein P02930 original sequence version: 126 6F97B4C62A848FE1 q9i1y8_pseae PAPS_reduct domain-containing protein PA2127 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MAGKHYQDADVHAATLSRLRLVFRNFERVCVAFSGGKDSSVTLQLALDVARELGRSPVDVLFIDLEGQYQATIDHVSEMLGRPDVRPWWVCLPLNLRNASSLEEPYWCCWEPGAEADWVRPLPKQRGVISDPAFFPFYRYRMEFEEFVAGFNAWLAREEPTAFLVGIRSDESLNRYLAVKRRSRAKQCAWTPPGGSAPLAWSARDRANPQAVSFFPIYDWRFEDLWRCVADHGYAYNRLYDQMYRAGVPFSQMRICQPYGDDQRKGLDLFHRIEPRTWFKVVRRVAGANYGARYCRQRFLGYRGGLGLPPSFGTWREYSQFLLRSMPPPLRGIYQRRIERFILWWKQHDYPLAIWPDAGIPALENRRKQPSWRRIALSLLKQDMARSLSFGFSQADIDRLVPGREKRS 87FD5B3B704643B1 mexb_pseae Multidrug resistance protein MexB Multidrug-efflux transporter MexB PA0426 mexB protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSKFFIDRPIFAWVIALVIMLAGGLSILSLPVNQYPAIAPPAIAVQVSYPGASAETVQDTVVQVIEQQMNGIDNLRYISSESNSDGSMTITVTFEQGTDPDIAQVQVQNKLQLATPLLPQEVQRQGIRVTKAVKNFLMVVGVVSTDGSMTKEDLSNYIVSNIQDPLSRTKGVGDFQVFGSQYSMRIWLDPAKLNSYQLTPGDVSSAIQAQNVQISSGQLGGLPAVKGQQLNATIIGKTRLQTAEQFENILLKVNPDGSQVRLKDVADVGLGGQDYSINAQFNGSPASGIAIKLATGANALDTAKAIRQTIANLEPFMPQGMKVVYPYDTTPVVSASIHEVVKTLGEAILLVFLVMYLFLQNFRATLIPTIAVPVVLLGTFGVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVMAEEGLSPREAARKSMGQIQGALVGIAMVLSAVFLPMAFFGGSTGVIYRQFSITIVSAMALSVIVALILTPALCATMLKPIEKGDHGEHKGGFFGWFNRMFLSTTHGYERGVASILKHRAPYLLIYVVIVAGMIWMFTRIPTAFLPDEDQGVLFAQVQTPPGSSAERTQVVVDSMREYLLEKESSSVSSVFTVTGFNFAGRGQSSGMAFIMLKPWEERPGGENSVFELAKRAQMHFFSFKDAMVFAFAPPSVLELGNATGFDLFLQDQAGVGHEVLLQARNKFLMLAAQNPALQRVRPNGMSDEPQYKLEIDDEKASALGVSLADINSTVSIAWGSSYVNDFIDRGRVKRVYLQGRPDARMNPDDLSKWYVRNDKGEMVPFNAFATGKWEYGSPKLERYNGVPAMEILGEPAPGLSSGDAMAAVEEIVKQLPKGVGYSWTGLSYEERLSGSQAPALYALSLLVVFLCLAALYESWSIPFSVMLVVPLGVIGALLATSMRGLSNDVFFQVGLLTTIGLSAKNAILIVEFAKELHEQGKGIVEAAIEACRMRLRPIVMTSLAFILGVVPLAISTGAGSGSQHAIGTGVIGGMVTATVLAIFWVPLFYVAVSTLFKDEASKQQASVEKGQ DIP protein P52002 original sequence version: 92 FF91855338868ED2 q9hwi4_pseae Histidine kinase PA4197 bfiS protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSPLPASPALNSLLRLLREGAPLVERVGALRRLLLEHPGTRQAWYLAWQPQAQTYTPVPPSPALPPGAGEPNRASDLALRERLVRDGRLALDELRRSASWLGARLRRAGVEHGMAFALDLQAGDEGLLLVASDTPQSAALDWLGLLLAPLLAAARGVTRAAPFLAADPQPALLLDGEAQAVELNQAFLALLGERPREAWRAYLPANHGQLVRASLGQARALGEVEAECDGRILLWQFIPDSAEARVLARCRDATASLRGEREAARASRLYRLITENTTDLISRHTLDGIFLDASPASWTLLGYWPEELRGRPAQALFHPQDRGQVALRAREALEQDGYLTITYRIRHRDGRYRWFETASRAIRETYTGAVVEVVSVSRDVTRRVEAEENRRRLAEVVEANTDLVLFVEHGGRVTYLNPSARAALGIADGQEAPALERLLAGDTPARLAEEGWRQARDGGVWSREGRLQPQDGRPSLPVSLVLLAHRGRGEERYYSLVARDMTERELREAQQRRHQDELAHTARLVTLGELASGIAHEINQPLAAVMNYASTSQRYLAVLGSQPEAAGRVAEGLARIGEHAGHAAEVIKRLRAFLRKGQRRLQALDLNQVAREAIGLCAWEAGHWQVAVEEAMTDNPPPLYADRVLLEQVFLNLLRNAIEANREAHPGSPSRVVIGSRVEPGGLLCLWVRDQGPGVPADQLEHIFTPFHTSKPEGLGLGLSMSRSIVEGFGGTLEAELPADGGLLMNCRLPLAAGATGG CB1BF1A2AE8E7144 bdla_pseae Biofilm dispersion protein BdlA bdlA Chemotaxis regulator BdlA PA1423 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MAALDRSMARVEFDPDGNITDANENFLTLLGYRRDEILGKPHRQLCDGAYAQSEDYRRFWERLRRGEHFSGRCKRITREGRPLWLEATYNPVRDGQGRLLKVVKYASDIDAIVHQEHEMQSKLDALSRSMAMIEFDLDGNVLAANDNFLATMGYGRAELASANHRQFCEPGYRDGPQYADLWRRLNRGEYVTGQFRRVHRNGQPVWLEASYNPVYDADGKLYKVVKFASDVSDRMRRYQAEADNAHQAHTLSTETRTVAEHGALIIQSAVEEMLKIANTLDASSLNIGELSQHSQQITSIVNTIREIAEQTNLLALNAAIEAARAGDQGRGFAVVADEVRQLAERTSKSTKEIADMIGRIQTGTRSVIDDMQHSQEQARRGVELANEAGAAILGIRESTHKVVEAVQQFSRTLNADL 266F998AA359843E q9huf2_pseae PA5017 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MKSHPDAASRSAAEVVTQLPVPSRLGLLRFERLNEPSWALLFLDPACERQLGLPATTLCALLDAPYASLMEPEARHRLHEQIQQQLVKRPHYQVSYKLHTPNGVLTMLEFGEAFQQHGRQLLHGYLMVEERAESAERSEQLLDLESQNLRLKASLDLYQRSQDDHLQHLLRSRTQQNLIVRLARHRYLSSDPLLEAAQLITQAACEAYGTARAGIWRLLDDQRLEAVTVYRRDLDQYEKPQSIDASRYPAYLEAVHSGRAIDAHNAQRDPRTQELYKDYLRPLGVNALLDATIRIGGEVVGVLCLEHAGENRMWQSDEIAFAGELADQYAQVLMNHERRNVSSALHLFQRAVEQSASAFLLIDRDGVVEYVNPSFTSITQYSADEVRNRRLSELPALENLSELLFDARSALTQQNSWQGEFRSRRKNHEPYWGQLSLSKVYDDLGELTHYIGIYEDITQNKLAQQHIEKLAYRDNLTGLANRHYFIGALEERLESSGDRPLSLLLVDIDNFKRINDSLGHQTGDKLLVSLARRLRSCLGDGATLARFASNEFAVLLDDTAVEKGESIAAQVLHMLDKPLFVDNQLINITGSIGLASAPQHGCDPQTLMKYAGLALHKAKANGKHQVQVFTEALTAEASYKLFVESNLRRALAQNELAVHYQPKLCLRSGQLLGLEALLRWQHPEKGMIRPDRFISVAEETGLIVPIGKWVIREACRQARELAEAGLGELQIAINLSPKQFTDPDLVGSIAAILHEENIPASQLELELTESLLLDATDDTRQQLERLKSLGLTLAMDDFGTGYSSLSYLKKFPIDVIKIDRSFIKDIPDSQDDMEITSAVIAMAHNLKLKVVAEGVESAEQLAFLRRNRCDIGQGYLFDRPIPSDLLNTSLLRYPCRTLH 925C1FA936731602 q9hwz4_pseae PA4033 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MGFRPVSQRLRDINLQALGKFSCLALVLGLESVSHPAGPVQAPSFSQGTASPSFATPLGLDGPARARAEMWNVGLSGAVSVRDELRWVF BFD4EBF98897E7E4 g3xcv7_pseae Peptidoglycan D,D-transpeptidase MrdA Penicillin-binding protein 2 mrdA PA4003 pbpA protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MPQPIHLKDHEKDARLVRRRVIVGAVAVVLLTLVLVARMYHLQVTQYEYHSTLSENNRVHVQPIPPTRGIIFDRNGVIIADNRPSFSLTITRERTEDLQKTLDTLVEILGLTEDDRAIFEKRMKQGRRPFEPVPIMFELNEEQIARIAVNQFRLPGVDVATQFVRHYPLKEHFAHSVGYVGRINEQELKNLDPINYSGTHHIGKTGIERFYESELHGTVGYEEVETNARGRVLRVLKRTDPIPGKDIVLSIDSRLQEAAENALAGRRGAIVAIQPSTGDVLAMVSQPSYDPNLFVTGISFKAYAELRDSIDRPLYNRVLRGLYPPGSTVKPAVALAGLDAGVVTPTSRVFDPGYYQLPNYDHKYRNWNRYGDGWVSLESAIYRSNDTYFYDLAHKLGIDRLHAFMSRFGFGQKVALDMFGEADGLMPSREWKRKTRRQVWYPGETLILGIGQGYMQATPIQLAQMTALLANKGHWIRPHLAKTIDGQPPVDPDPMPDIVLRDPANWDRVDYGMQQVVHGARGTARKVGATSAYLIAGKSGTAQVVAIKQNERYDRSKLLERHRDHALFVGFAPANNPQIAVAVMVENGESGSGVAAPVVKQVMDAWLLDEHGKLKAEYAEPVAPLAAAVAKPEPTAAEPEAPALEQ 2F4CA6F5746CCCB1 q9i019_pseae Histidine kinase PA2824 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MLGGRTSPRLIPAPMDIALTHRLSFKQASLTVLVAFILGTLLSLIQVGVDYASQDASINREVRALLDVSHNPAARIAYNIDAELAQELVLGLLRSPAVVRAEIIDTSGLPLASASREPAESRLRPLSDFLFGHKRVYEDPLHVDHAPGEALGVLHLEIDTFVFGNDFLRRAGITLLSGFVRSLLLSLILLVLFYTLLTKPLVSLIQALSGHDPRSPARMRLPCPKGHERDEIGVLVEVINRQLGRISVEIEQRREAENRLTQYLEELESIVAARTAELKAANARLTLSNQELEEARQTALDMAQARASFLANMSHEIRTPLNGLLGMLSLSLDGPLTPEQRQQLSIAHDSGKVLVELLNDVLDLSKFEAGQLVLEQIPFDLGVLVEDTASLLSQNAAAGVELTCLVDPALPAQVSGDPTRIRQIVSNLLSNALKFTRLGRVDVRVEATAEGVRISVRDTGIGIAQEALDRIFQPFTQADAGITRQYGGTGLGLALTRKLCEAMQGELTVESTVGLGSLFSVGLPLAPVSPPLQALPLRGRVIAQCSANSGLAQLLQTWLPRWGLEYKRLETDDSLLGHSLDVLISDCPDCLMGLRPSIGTPILLVTAYGSFLEPELARRLSPLRQLARPLSRNQLYQALKHVLEHTAIAPSSASDTTGEQRNTRVLLVEDNPVNQLVAKGLLHKLGCQVWIAEHGLNALKMLEEHPIDLVLMDCNMPVMDGYEATRQIRDSGRWGGLPIIALTANALPDERERCRAAGMDDYLAKPFHRDELKAILDRWCPLTASD 3B134513F3538F7C g3xcz3_pseae pilZ PA2960 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSLPPNLGPRNGILSLTIKDKSVLYAAYMPFIRNGGLFIPTNKNYKLGDEVFMLLNLMEEPEKIPVAGKVVWITPKGAQGNRAAGIGVQFNDGDNTARNKIETYLAGALKSDRPTHTM 55F357D2C752308D spot_ecoli Bifunctional (p)ppGpp synthase/hydrolase SpoT spoT b3650 JW3625 protein protein ecoli Escherichia coli (strain K12) MYLFESLNQLIQTYLPEDQIKRLRQAYLVARDAHEGQTRSSGEPYITHPVAVACILAEMKLDYETLMAALLHDVIEDTPATYQDMEQLFGKSVAELVEGVSKLDKLKFRDKKEAQAENFRKMIMAMVQDIRVILIKLADRTHNMRTLGSLRPDKRRRIARETLEIYSPLAHRLGIHHIKTELEELGFEALYPNRYRVIKEVVKAARGNRKEMIQKILSEIEGRLQEAGIPCRVSGREKHLYSIYCKMVLKEQRFHSIMDIYAFRVIVNDSDTCYRVLGQMHSLYKPRPGRVKDYIAIPKANGYQSLHTSMIGPHGVPVEVQIRTEDMDQMAEMGVAAHWAYKEHGETSTTAQIRAQRWMQSLLELQQSAGSSFEFIESVKSDLFPDEIYVFTPEGRIVELPAGATPVDFAYAVHTDIGHACVGARVDRQPYPLSQPLTSGQTVEIITAPGARPNAAWLNFVVSSKARAKIRQLLKNLKRDDSVSLGRRLLNHALGGSRKLNEIPQENIQRELDRMKLATLDDLLAEIGLGNAMSVVVAKNLQHGDASIPPATQSHGHLPIKGADGVLITFAKCCRPIPGDPIIAHVSPGKGLVIHHESCRNIRGYQKEPEKFMAVEWDKETAQEFITEIKVEMFNHQGALANLTAAINTTTSNIQSLNTEEKDGRVYSAFIRLTARDRVHLANIMRKIRVMPDVIKVTRNRN A85F70F57D082EE8 A85F70F57D082EE8 acp_ecoli Acyl carrier protein acpP b1094 JW1080 Cytosolic-activating factor Fatty acid synthase acyl carrier protein protein protein ecoli Escherichia coli (strain K12) MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEAEKITTVQAAIDYINGHQA DIP protein P0A6A8 original sequence version: 43 DIP protein P0A6A8 original sequence version: 56 DIP protein P0A6A8 original sequence version: 86 41FCFC39D45BFEA1 q8pjx9_xanac XAC2398 protein protein xanac Xanthomonas axonopodis pv. citri (strain 306) MQKGKDLTLRLMIVDDSVESAETIVTALRNGGIAVRPSRPQSQEELASMLSGQIDLAILGQAQQIPMSALQTQIAGSGKDIPILLLAERIEENALVEAASHGVRAIALRHRPAHLLALVRSEWDDLQARRGLRRIEAQMRETERRCDALIASSRDPIAYVHEGMHIRANDAYLEMFGFESFDDVEGISLLDMIAAQYVDDFKQLLKAMSKGEPPPAQYKLDARRVEGDTFPATMEFATATYEGEPCIQVVFRRREEFDPELAREVEDLRQRDQVTGLLNRPTFMVALEQAVAQAGRSEGQSGFLLIEPDHYARILPEFGLDSADALIAALAAHVASVLDDSVLAARFGEHSFALLLNGNYARTHALAETVRNAFAQHVFSVGTRSATVTVSIGGVQIGEKIASIGQVLNRGTEAVRTTAELGGNAVSIYDPAAADRAEEERIERWVEQLREALVGDGFLLHYQPVLNLQGEPLELYQAFLRLERNGEMMSPNAFMAIAEEHDLVTEIDRWVVARAIRQLGERQRAGHKTHLLVRIGPNSFSDPQMIDTIREQLAVYGVPGERLWLQTPESKVFTHLRNAQQFLAAVSAMDCKVGLEQFGSGLDSFQLLAHFHPAFLKLDRGITGDIASARDSQEKIREITSRAQPAGILTMAEFVADAQSMSSFFSAGVDYVQGDFVAPTGPLMNYEFG 9477086E930FCC4A q9hx24_pseae PA4001 sltB1 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MKNAMQVLRTWAARGVQWVGVAGVIGLSGAAQAGDYDGSPQVAEFVSEMTRDYGFAGEQLMGLFRDVNRKQSILDAISRPAERVKQWKEYRPIFISDARISRGVDFWNKHAEDLARAEKEYGVPAEIIVSIIGVETFFGRNTGSYRVMDALSTLGFDYPPRADFFRKELREFLLLAREQQVDPLSLTGSYAGAMGLPQFMPSSFRAYAVDFDGDGHINIWSDPTDAIGSVASYFKQHGWVTGEPVVSVAEINDESAESAVTRGVDPTMSLGELRARGWRTHDALRDDQKVTAMRFVGDKGIEYWVGLPNFYVITRYNRSAMYAMAVYQLAGEIARARGAH 7A00BD23A0695BD8 mexa_pseae Multidrug resistance protein MexA mexA PA0425 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MQRTPAMRVLVPALLVAISALSGCGKSEAPPPAQTPEVGIVTLEAQTVTLNTELPGRTNAFRIAEVRPQVNGIILKRLFKEGSDVKAGQQLYQIDPATYEADYQSAQANLASTQEQAQRYKLLVADQAVSKQQYADANAAYLQSKAAVEQARINLRYTKVLSPISGRIGRSAVTEGALVTNGQANAMATVQQLDPIYVDVTQPSTALLRLRRELASGQLERAGDNAAKVSLKLEDGSQYPLEGRLEFSEVSVDEGTGSVTIRAVFPNPNNELLPGMFVHAQLQEGVKQKAILAPQQGVTRDLKGQATALVVNAQNKVELRVIKADRVIGDKWLVTEGLNAGDKIITEGLQFVQPGVEVKTVPAKNVASAQKADAAPAKTDSKG 0D161F917B3529F2 acp1_pseae Acyl carrier protein 1 acpP1 acpP PA2966 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSTIEERVKKIVAEQLGVKEEEVTNSASFVEDLGADSLDTVELVMALEEEFETEIPDEKAEKITTVQEAIDYIVAHQQ 77F95B04F25E1348 pscg_pseae Type III export protein PscG Pseudomonas secretion protein G PA1720 pscG protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MDTSLIRELAELALAGSGQHCHEEALCIAEWLERLGQDEAARLIRISSLANQGRYQEALAFAHGNPWPALEPWFALCEWHLGLGAALDRRLAGLGGSSDPALADFAAGMRAQVRT DIP protein P95435 original sequence version: 75 3F546AA0645050B7 exsd_pseae Transcriptional antiactivator ExsD exsD PA1714 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MEQEDDKQYSREAVFAGRRVSVVGSDARSRGRVPGYASSSLYRESGIISARQLALLQRMLPRLRLEQLFRCEWLQQRLARGLALGREEVRQILLCAAQDDDGWCSELGDRVNLAVPQSMIDWVLLPVYGWWESLLDQAIPGWRLSLVELETQSRQLRVKSEFWSRVAELEPEQAREELARVAKCQARTQEQVAELAGKLETASALAKSAWPNWQRGMATLLASGGLAGFEPIPEVLECLWQPLCRLDDDVGAADAVQAWLHERNLCQAQDHFYWQS A6C56685A704124A q9htm0_pseae Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase Penta-phosphate guanosine-3'-pyrophosphohydrolase PA5338 spoT protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MPGIDAFADRLSSYLGPDQVNLVRRAYYYAEQAHDGQRRRSGEPYVTHPLAVSNILADMHMDHQSLMAAMLHDVIEDTGIAKEALTAQFGETVSELVDGVSKLTQMNFETKAEAQAENFQKMAMAMARDIRVILVKLADRLHNMRTLEVLSGEKRRRIAKETLEIYAPIANRLGMHTMRVEFEDLGFKAMHPMRAERIRQAVKKARGNRREIVGKIQESLVNCLAREGMEGQVIGREKHLYSIYQKMRGKRKAFNEIMDVYAFRIIVDKVDTCYRVLGAVHSLYKPFPGRFKDYIAIPKANGYQSLHTTLFGMHGVPIEIQIRTREMEEMANHGIAAHWLYKSNDETPKGTHARARQWVKGVLELQQRAGNSLEFIENVKIDLFPDEVYVFTPKGRIMELPKGSTAVDFAYAVHTDVGNSCIACRINRRLAPLSEPLQSGQTVEIVTAPGARPNPAWLSFVVTGKARTHIRHALKLQRRSESINLGERLLNKTLTGFDSHLEKIPQERIQAVLAEYRMEVFEDLLEEIGLGNRMAYVVARRLLSSEGEEAPSAEGPLAIRGTEGLVLSYAKCCTPIPGDPIVGHLSAGKGMVVHLESCKNISEVRHNPEKCIQLSWAKDVTGEFNVELRVELEHQRGLIALLATSVNAADGNIEKISMDERDGRISVVQLVVSVHDRVHLARVIKKLRALKGVIRITRLRS 6F94E4A2CB2A4FC5 vfr_pseae cAMP-activated global transcriptional regulator Vfr vfr PA0652 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MVAITHTPKLKHLDKLLAHCHRRRYTAKSTIIYAGDRCETLFFIIKGSVTILIEDDDGREMIIGYLNSGDFFGELGLFEKEGSEQERSAWVRAKVECEVAEISYAKFRELSQQDSEILYTLGSQMADRLRKTTRKVGDLAFLDVTGRVARTLLDLCQQPDAMTHPDGMQIKITRQEIGRIVGCSREMVGRVLKSLEEQGLVHVKGKTMVVFGTR 03B7F2A4C2CED7E6 exsa_pseae HTH-type transcriptional regulator ExsA exsA PA1713 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MQGAKSLGRKQITSCHWNIPTFEYRVNKEEGVYVLLEGELTVQDIDSTFCLAPGELLFVRRGSYVVSTKGKDSRILWIPLSAQFLQGFVQRFGALLSEVERCDEPVPGIIAFAATPLLAGCVKGLKELLVHEHPPMLACLKIEELLMLFAFSPQGPLLMSVLRQLSNRHVERLQLFMEKHYLNEWKLSDFSREFGMGLTTFKELFGSVYGVSPRAWISERRILYAHQLLLNSDMSIVDIAMEAGFSSQSYFTQSYRRRFGCTPSRSRQGKDECRAKNN 4823D0E9135E0BB7 fmpa_pseai Fimbrial protein pilA fimA Pilin protein protein pseai Pseudomonas aeruginosa MKAQKGFTLIELMIVVAIIGILAAIAIPQYQNYVARSEGASALASVNPLKTTVEEALSRGWSVKSGTGTEDATKKEVPLGVAADANKLGTIALKPDPADGTADITLTFTMGGAGPKNKGKIITLTRTAADGLWKCTSDQDEQFIPKGCSR C0E35B69FD6FBE84 acp2_pseae Acyl carrier protein 2 acpP2 PA1869 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MDDIETRVRKLVAARFGVEECDIRLDSDFRNDFGAESLEVVELVMALEAEFGVEIADDDAERIETVRQAIDYLEEAVPT A7D384788CE81ABA q9i580_pseae PA0861 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MRQNRTLDKPRLLGLVWPFIVVVLLQAMLAGGSLYVLSAVRSYVGGESLWSKGQKDAIYYLTLYADSRADEDFRRYEEAIAIPLGDREMRLALDQPDPDIEAARQGILKGGNHADDVTAIIWLYRNFHDFSYFERAIELWLVGDKYVMELIDVAGKMRAGIGTGQASAEQVQQWKTEIHAINEKVTPAAKAFSDALGEGSRALLRLLLVANLTTASVLILLAFLRTRQQLMQRQEVENALDAERERAQITLASIGDGVITADTQGGISYLNPAAEQMTNWTLDKARGLPLASLFRIVDESSREEGMLLIEQILSGEIDGGREHSKLVLRHDGSSVPVTLVGAPIHRGAEITGVVLVLHDMTRERQYMARLSWQATHDALTGLTNRREFEYRLQIALERLERNSGRHALMFLDLDQFKLVNDTCGHAAGDELLRQVCTLLQQGLREGDTLARLGGDEFGILLENCPAEKAVEIADHLRKTIQDLHFTWSGQPFNCTVSVGLVHLLPGISTLEEALRSADMACYMAKEKGRNRVQVFHQDDVELSMRFGEMTWVQRIHLALEEDRFSLYAQPIVPLGEGAEEGLHVELLLRLRDEGGRLVPPLSFIPAAERYGLMTLIDRWVVENAFRTLVERAQDPRAEPIGTCAINLSGATIGDESFLQFLTELFARYRIPPQTICFEVTETVAVANLASAIRFINELKDTGCRFSLDDFCAGMSSFIYLKHLPVDYLKIDGSFVKDMLEDPIDRAMVQVINHIGHVMGKRTIAEFVETVEVMEALREIGIDYAQGLAIGAPLPFSRQPPGAGVDAQGLWSSLGQNLR 8DB0837DCA13C31F muca_pseae Sigma factor AlgU negative regulatory protein mucA PA0763 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSREALQETLSAVMDNEADELELRRVLAACGEDAELRSTWSRYQLARSVMHREPTLPKLDIAAAVSAALADEAAPPKAEKGPWRMVGRLAVAASVTLAVLAGVRLYNQNDALPQMAQQGTTPQIALPQVKGPAVLAGYSEEQGAPQVITNSSSSDTRWHEQRLPIYLRQHVQQSAVSGTESALPYARAASLENR 421755F4F113769B q9i1y9_pseae ParB domain-containing protein PA2126 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MAQTKTLTERAEALFGELHGLPLAERIEAINRIRRLLHAHSPFAEEPVDCVQWVRAERVAGNDYNPNTVAPPEMRLLRLSIESDGFTQPIVAYPQADGRYEVVDGFHRLRVGSAKGALRQRLHGYLPIAAIRAGREGDSERIAATIRHNRARGVHGVLPMTAIVVTLLKAGWSEADVARELGMDNDEVLRFKQVSGLPELFREHVYSRSWE 03D4227BD4245390 armr-mexr 15 36 unspecified role unspecified role prey prey P52003:p.Leu35Pro P52003-35-35 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L P Wed May 02 14:38:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu35pro' Tue Jun 30 16:19:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu35Pro' P52003:p.Ile104Phe P52003-104-104 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain I F Wed May 02 17:26:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile104phe' Tue Jun 30 20:09:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile104Phe' P52003:p.Leu75Pro P52003-75-75 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L P Wed May 02 17:06:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu75pro' Tue Jun 30 17:30:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu75Pro' P52003:p.Met112Thr P52003-112-112 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain M T Wed May 02 15:25:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'met112thr' Tue Jun 30 18:15:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Met112Thr' P52003:p.Leu135Pro P52003-135-135 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L P Wed May 02 19:08:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu135pro' Tue Jun 30 19:28:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu135Pro' P52003:p.Leu28Pro P52003-28-28 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L P Wed May 02 20:07:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu28pro' Tue Jun 30 18:16:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu28Pro' 32 unspecified role unspecified role bait bait region Q9HXS2-25-53 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9HXS2:p.Trp45Ala Q9HXS2-45-45 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain W A Wed May 02 17:33:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp45ala' Tue Jun 30 16:04:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp45Ala' Q9HXS2:p.Leu36Ala Q9HXS2-36-36 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L A Wed May 02 19:01:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu36ala' Tue Jun 30 19:53:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu36Ala' physical association physical association table 2 mexb-mexa 20 47 unspecified role unspecified role bait bait region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P52002:p.Gly220Ser mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain G S Wed May 02 14:43:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly220ser' Tue Jun 30 15:43:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly220Ser' 59 unspecified role unspecified role prey prey P52477:p.Val259Phe mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain V F Wed May 02 17:11:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val259phe' Tue Jun 30 17:07:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val259Phe' P52477:p.Val66Met mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain V M Wed May 02 16:57:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val66met' Tue Jun 30 18:23:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val66Met' physical association physical association Fig. 2 arca-mexb 10 44 unspecified role unspecified role neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 47 unspecified role unspecified role neutral component neutral component physical association physical association Fig. 1A arca-mexb-1 10 44 unspecified role unspecified role bait bait region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 45 unspecified role unspecified role prey prey 47 unspecified role unspecified role prey prey association association Figs. 1B, 4 sltb1-mrca-3 3 52 unspecified role unspecified role prey prey region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli 58 unspecified role unspecified role bait bait ecolx Escherichia coli physical association physical association Fig. 3 sltb1-mrca-2 9 52 unspecified role unspecified role prey prey region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli 58 unspecified role unspecified role bait bait ecolx Escherichia coli direct interaction direct interaction Fig 4 rpod-rpod-5 8 43 unspecified role unspecified role bait bait region 4 sufficient to bind sufficient binding region sufficient to bind range range certain certain sequence position certain 43 unspecified role unspecified role prey prey region 2 sufficient to bind sufficient binding region sufficient to bind range range range range 35 unspecified role unspecified role ancillary ancillary physical association physical association Fig. 5 rela-rela-8 23 33 unspecified role unspecified role bait bait 33 unspecified role unspecified role prey prey physical association physical association in text spot-spot-1 23 63 unspecified role unspecified role bait bait 63 unspecified role unspecified role prey prey physical association physical association in text acpp2-spot 23 63 unspecified role unspecified role prey prey 67 unspecified role unspecified role bait bait o52658-- O52658-- flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association figure 5 acpp2-spot-1 23 55 unspecified role unspecified role prey prey 67 unspecified role unspecified role bait bait o52658-- O52658-- flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association figure 5 acpp1-spot 23 60 unspecified role unspecified role bait bait o54439-- O54439-- flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 63 unspecified role unspecified role prey prey physical association physical association figure 5 acpp1-spot-1 23 55 unspecified role unspecified role prey prey 60 unspecified role unspecified role bait bait o54439-- O54439-- flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association figure 5 acpp-spot 23 56 unspecified role unspecified role bait bait p0a6a8-- P0A6A8-- flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 63 unspecified role unspecified role prey prey physical association physical association figure 5 muca-mucb 22 69 unspecified role unspecified role bait bait n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 34 unspecified role unspecified role prey prey pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) physical association physical association Fig. 1 mucb-mucb 4 34 unspecified role unspecified role neutral component neutral component c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 34 unspecified role unspecified role neutral component neutral component c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 150 147 direct interaction direct interaction Fig. 6C algw-muca 26 69 enzyme target enzyme target substrate substrate neutral component neutral component n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 37 enzyme enzyme neutral component neutral component n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli cleavage cleavage reaction cleavage Fig. 1 muca-mucb-1 4 69 unspecified role unspecified role neutral component neutral component periplasmic region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 34 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecolx Escherichia coli 163 160 direct interaction direct interaction Fig. 6C clpv1-fha1 16 28 unspecified role unspecified role prey prey 38 enzyme enzyme bait bait c-terminal tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged c-term range C-terminal range c-term range c-term range C-terminal range c-term range physical association physical association The association of these proteins did not strictly require PpkA, though the kinase reproducibly enhanced the association. Fig. 3D exsa-exsa-1 11 65 unspecified role unspecified role unspecified role unspecified role region P26993-- lexa dna bd lexa dna binding domain lexa dna bd undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 65 unspecified role unspecified role unspecified role unspecified role p26993-- P26993-- lexa dna bd lexa dna binding domain lexa dna bd undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Fig. 6A exsc-exsd-1 25 42 unspecified role unspecified role bait bait region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 62 unspecified role unspecified role prey prey physical association physical association Fig. 3A psce-pscg 21 31 unspecified role unspecified role bait bait Q9I317:p.Leu20Ser Q9I317-20-20 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L S Wed May 02 16:24:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu20ser' Tue Jun 30 16:46:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu20Ser' q9i317-- Q9I317-- his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q9I317:p.Gly57Asp Q9I317-57-57 mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain G D Wed May 02 15:11:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly57asp' Tue Jun 30 18:48:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly57Asp' 61 unspecified role unspecified role prey prey P95435:p.[Ile28Ser;Trp31Ser] P95435-28-31 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain I S certain certain sequence position certain certain certain sequence position certain W S Wed May 02 16:52:32 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile28ser,trp31ser' Tue Jun 30 15:54:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ile28Ser;Trp31Ser]' P95435:p.Leu5Ser P95435-5-5 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L S Wed May 02 20:01:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu5ser' Tue Jun 30 19:29:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu5Ser' P95435:p.[Leu5Ser;Leu9Ser] P95435-5-9 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L S certain certain sequence position certain certain certain sequence position certain L S Fri Jul 22 11:00:02 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'leu9ser,leu5ser' Wed May 02 15:52:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu5ser,leu9ser' Tue Jun 30 19:33:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu5Ser;Leu9Ser]' P95435:p.Ile28Ser P95435-28-28 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain I S Wed May 02 15:36:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile28ser' Tue Jun 30 20:12:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile28Ser' P95435:p.Leu9Ser P95435-9-9 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L S Wed May 02 17:46:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu9ser' Tue Jun 30 19:44:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu9Ser' physical association physical association Figure 2 phzr-phzr-1 24 39 unspecified role unspecified role neutral component neutral component physical association physical association figure 3 spooj-spooj 12 40 unspecified role unspecified role unspecified role unspecified role q9ht12-- Q9HT12-- his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region Q9HT12-250-290 required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain physical association physical association figure 3A spooj-spooj-1 27 40 unspecified role unspecified role unspecified role unspecified role Q9HT12:p.Gly71Asp Q9HT12-71-71 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain G D Wed May 02 14:47:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly71asp' Tue Jun 30 16:11:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly71Asp' Q9HT12:p.Ala158Val Q9HT12-158-158 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain A V Wed May 02 18:02:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala158val' Tue Jun 30 16:32:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala158Val' q9ht12-- Q9HT12-- his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q9HT12:p.Arg94Cys Q9HT12-94-94 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R C Wed May 02 19:03:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg94cys' Tue Jun 30 16:20:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg94Cys' region Q9HT12-250-290 required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain Q9HT12:p.Ala97Thr Q9HT12-97-97 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain A T Wed May 02 19:15:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala97thr' Tue Jun 30 17:42:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala97Thr' Q9HT12:p.Pro107Ser Q9HT12-107-107 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain P S Wed May 02 18:56:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro107ser' Tue Jun 30 17:44:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro107Ser' Q9HT12:p.Gly47Asp Q9HT12-47-47 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain G D Wed May 02 17:12:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly47asp' Tue Jun 30 16:59:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly47Asp' physical association physical association Figure 3B and table 4 vfr-vfr 14 64 unspecified role unspecified role unspecified role unspecified role region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association figure 2 2.8A Rworking = 0.19 Rfree = 0.25 q9i1y9_pseae-q9i1y9_pseae-1 17 70 unspecified role unspecified role prey prey region Q9I1Y9-2-87 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9I1Y9:p.Leu197Ser Q9I1Y9-197-197 mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain L S Wed May 02 14:44:26 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu197ser' Tue Jun 30 16:48:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu197Ser' 70 unspecified role unspecified role bait bait q9i1y9-88-211 Q9I1Y9-88-211 required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain physical association physical association Figure 1 q9i1y9-q9i1y8 17 46 unspecified role unspecified role prey prey region Q9I1Y8-2-247 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 70 unspecified role unspecified role bait bait region Q9I1Y9-170-211 required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain Q9I1Y9:p.Leu197Ser Q9I1Y9-197-197 mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain L S Wed May 02 18:58:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu197ser' Tue Jun 30 17:12:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu197Ser' physical association physical association figure 1 q9i1y8-q9i1y9 5 46 unspecified role unspecified role bait bait q9i1y8-- Q9I1Y8-- tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 70 unspecified role unspecified role prey prey Q9I1Y9:p.Leu197Ser Q9I1Y9-197-197 mutation mutation certain certain sequence position certain certain certain sequence position certain L S Wed May 02 15:27:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu197ser' Tue Jun 30 20:24:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu197Ser' physical association physical association figure 4 bfis-q9i019 6 53 unspecified role unspecified role prey prey q9i019-- Q9I019-- ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 48 unspecified role unspecified role bait bait q9hwi4-- Q9HWI4-- his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association figure 7C q9i019-bfir 6 53 unspecified role unspecified role bait bait q9i019-- Q9I019-- ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 29 unspecified role unspecified role prey prey q9hwi5-- Q9HWI5-- his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association figure 7B arga-arga 2 30 unspecified role unspecified role unspecified role unspecified role physical association physical association figure 4c q9huf2-bdla 18 49 unspecified role unspecified role prey prey region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q9I3S1:p.Gly31Ala Q9I3S1-31-31 mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain G A Wed May 02 16:27:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly31ala' Tue Jun 30 18:16:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly31Ala' 50 unspecified role unspecified role bait bait region v5 tag v5 tag GKPIPNPLLGLDST epitope tag GKPIPNPLLGLDST epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association figure 8 q9i580-bdla 18 49 unspecified role unspecified role prey prey region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q9I3S1:p.Gly31Ala Q9I3S1-31-31 mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain G A Wed May 02 19:29:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly31ala' Tue Jun 30 16:52:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly31Ala' 68 unspecified role unspecified role bait bait region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region v5 tag v5 tag GKPIPNPLLGLDST epitope tag GKPIPNPLLGLDST epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association figure 8 pilz-q8pjx9-9 13 57 unspecified role unspecified role neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region Q8PJX9-436-689 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 54 unspecified role unspecified role neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 3c pila-xcpt-1 7 41 unspecified role unspecified role prey prey 66 unspecified role unspecified role bait bait physical association physical association Fig. 4A, 4B xcpt-xcpt 7 41 unspecified role unspecified role neutral component neutral component 41 unspecified role unspecified role neutral component neutral component physical association physical association Fig. 5 arga-1 2 30 unspecified role unspecified role unspecified role unspecified role region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association figure 6 armr-mexr-1 19 36 unspecified role unspecified role neutral component neutral component P52003:p.Ile104Phe mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain I F Wed May 02 16:31:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile104phe' Tue Jun 30 17:17:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile104Phe' ecolx Escherichia coli 32 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli direct interaction direct interaction Fig. 1 algw-muca-1 26 51 stimulator stimulator unspecified role unspecified role region sufficient to bind sufficient binding region sufficient to bind undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined chemical synthesis Chemical synthesis (Chemical synthesis) 37 enzyme enzyme neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 69 enzyme target enzyme target substrate substrate neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association Fig. 1 muca-mucb-2 1 69 unspecified role unspecified role neutral component neutral component region fluor-5-maleimide fluorescein-5-maleimide label fluor-5-maleimide undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P38107:p.Ser154Cys mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain S C Wed May 02 15:54:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser154cys' Tue Jun 30 17:48:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser154Cys' periplasmic region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 34 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli direct interaction direct interaction Fig. 6B algw-muca-2 26 37 enzyme enzyme neutral component neutral component n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 69 enzyme target enzyme target substrate substrate neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 34 inhibitor inhibitor unspecified role unspecified role ecolx Escherichia coli cleavage cleavage reaction cleavage Fig. 1 exsa-exsd 25 65 unspecified role unspecified role bait bait region P26993-- his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 62 unspecified role unspecified role prey prey physical association physical association Fig. 3 exsa-exsd-1 11 65 unspecified role unspecified role unspecified role unspecified role region P26993-- lexa dna bd lexa dna binding domain lexa dna bd undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 62 unspecified role unspecified role unspecified role unspecified role region lexa dna bd lexa dna binding domain lexa dna bd undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Fig. 6A MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Subcellular localization of the pyoverdine biogenesis machinery of Pseudomonas aeruginosa: a membrane-associated "siderosome" Subcellular localization of the pyoverdine biogenesis machinery of Pseudomonas aeruginosa: a membrane-associated "siderosome" FEBS Lett. (0014-5793) 2013 imex curation Imperi F., Visca P. paolo.visca@uniroma3.it 30-Sept-2013: Contacted by IntAct-Help. Only protein-protein interactions pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) confocal microscopy confocal microscopy tag fluorescence tag visualisation by fluorescence tag fluorescence Imperi F., Visca P. paolo.visca@uniroma3.it Accepted 2013-AUG-28 by LPERFETTO 30-Sept-2013: Contacted by IntAct-Help. FEBS Lett. (0014-5793) 2013 Only protein-protein interactions imex curation Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. FEBS letters 2016 imex curation Aguirre C., Goto Y., Costas M. gtyj8126@protein.osaka-u.ac.jp 11-Apr-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro dsc differential scanning calorimetry dsc predetermined predetermined participant predetermined Aguirre C., Goto Y., Costas M. gtyj8126@protein.osaka-u.ac.jp Accepted 2016-MAR-31 AT 09:30 BST AT 09:30 BST by MARTA FEBS letters 2016 Only protein-protein interactions imex curation imex curation Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. FEBS letters 2016 imex curation Aguirre C., Goto Y., Costas M. gtyj8126@protein.osaka-u.ac.jp 11-Apr-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro uv-vis ultraviolet-visible spectroscopy uv-vis predetermined predetermined participant predetermined Aguirre C., Goto Y., Costas M. gtyj8126@protein.osaka-u.ac.jp Accepted 2016-MAR-31 AT 09:30 BST AT 09:30 BST by MARTA FEBS letters 2016 Only protein-protein interactions imex curation imex curation An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. FEBS letters 2015 imex curation An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr 03-Dec-2015: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro bn-page blue native page bn-page weight by staining molecular weight estimation by staining weight by staining An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr Accepted 2015-NOV-09 AT 14:19 GMT AT 14:19 GMT by LUANA FEBS letters 2015 Only protein-protein interactions imex curation imex curation Probing the reactivity of different forms of azurin by flavin photoreduction. Probing the reactivity of different forms of azurin by flavin photoreduction. FEBS J. (1742-464X) 2011 Alagaratnam S., Meeuwenoord NJ., Navarro JA., Hervás M., De la Rosa MA., Hoffmann M., Einsle O., Ubbink M., Canters GW. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Alagaratnam S., Meeuwenoord NJ., Navarro JA., Hervás M., De la Rosa MA., Hoffmann M., Einsle O., Ubbink M., Canters GW. FEBS J. (1742-464X) 2011 Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. FEBS letters 2016 imex curation Aguirre C., Goto Y., Costas M. gtyj8126@protein.osaka-u.ac.jp 11-Apr-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Aguirre C., Goto Y., Costas M. gtyj8126@protein.osaka-u.ac.jp Accepted 2016-MAR-31 AT 09:30 BST AT 09:30 BST by MARTA FEBS letters 2016 Only protein-protein interactions imex curation imex curation Subcellular localization of the pyoverdine biogenesis machinery of Pseudomonas aeruginosa: a membrane-associated "siderosome" Subcellular localization of the pyoverdine biogenesis machinery of Pseudomonas aeruginosa: a membrane-associated "siderosome" FEBS Lett. (0014-5793) 2013 imex curation Imperi F., Visca P. paolo.visca@uniroma3.it 30-Sept-2013: Contacted by IntAct-Help. Only protein-protein interactions pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) pull down pull down de novo protein sequence de novo protein sequencing by mass spectrometry de novo protein sequence Imperi F., Visca P. paolo.visca@uniroma3.it Accepted 2013-AUG-28 by LPERFETTO 30-Sept-2013: Contacted by IntAct-Help. FEBS Lett. (0014-5793) 2013 Only protein-protein interactions imex curation Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi-functional c-di-GMP regulator. Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi-functional c-di-GMP regulator. FEBS Lett. (0014-5793) 2014 imex curation Phippen C.W., Mikolajek H., Schlaefli H.G., Keevil C.W., Webb J.S., Tews I. Ivo.Tews@soton.ac.uk 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Phippen C.W., Mikolajek H., Schlaefli H.G., Keevil C.W., Webb J.S., Tews I. Ivo.Tews@soton.ac.uk Accepted 2015-FEB-11 by LUANA FEBS Lett. (0014-5793) 2014 Only protein-protein interactions imex curation An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. FEBS letters 2015 imex curation An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr 03-Dec-2015: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr Accepted 2015-NOV-09 AT 14:19 GMT AT 14:19 GMT by LUANA FEBS letters 2015 Only protein-protein interactions imex curation imex curation Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR. Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR. EMBO Rep. (1469-221X) 2010 imex curation Chen H., Yi C., Zhang J., Zhang W., Ge Z., Yang CG., He C. chenhao@nju.edu.cn Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Chen H., Yi C., Zhang J., Zhang W., Ge Z., Yang CG., He C. chenhao@nju.edu.cn EMBO Rep. (1469-221X) 2010 Only protein-protein interactions imex curation Subcellular localization of the pyoverdine biogenesis machinery of Pseudomonas aeruginosa: a membrane-associated "siderosome" Subcellular localization of the pyoverdine biogenesis machinery of Pseudomonas aeruginosa: a membrane-associated "siderosome" FEBS Lett. (0014-5793) 2013 imex curation Imperi F., Visca P. paolo.visca@uniroma3.it 30-Sept-2013: Contacted by IntAct-Help. Only protein-protein interactions ecoli Escherichia coli (strain K12) 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Imperi F., Visca P. paolo.visca@uniroma3.it Accepted 2013-AUG-28 by LPERFETTO 30-Sept-2013: Contacted by IntAct-Help. FEBS Lett. (0014-5793) 2013 Only protein-protein interactions imex curation Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. FEBS letters 2016 imex curation Aguirre C., Goto Y., Costas M. gtyj8126@protein.osaka-u.ac.jp 11-Apr-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro bn-page blue native page bn-page weight by comassie molecular weight estimation by coomasie staining weight by comassie Aguirre C., Goto Y., Costas M. gtyj8126@protein.osaka-u.ac.jp Accepted 2016-MAR-31 AT 09:30 BST AT 09:30 BST by MARTA FEBS letters 2016 Only protein-protein interactions imex curation imex curation Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. FEBS letters 2016 imex curation Aguirre C., Goto Y., Costas M. gtyj8126@protein.osaka-u.ac.jp 11-Apr-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro cd circular dichroism CD CD cd predetermined predetermined participant predetermined Aguirre C., Goto Y., Costas M. gtyj8126@protein.osaka-u.ac.jp Accepted 2016-MAR-31 AT 09:30 BST AT 09:30 BST by MARTA FEBS letters 2016 Only protein-protein interactions imex curation imex curation Evidence for self-association of the alternative sigma factor σ54. Evidence for self-association of the alternative sigma factor σ54. FEBS J. (1742-464X) 2013 Sabbatini M., Vezzoli A., Milani M., Bertoni G. suggested by lperfetto yeast Saccharomyces cerevisiae Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Sabbatini M., Vezzoli A., Milani M., Bertoni G. suggested by lperfetto FEBS J. (1742-464X) 2013 Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond. Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond. J. Biol. Chem. (0021-9258) 2001 Hege T., Feltzer RE., Gray RD., Baumann U. no in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Hege T., Feltzer RE., Gray RD., Baumann U. no J. Biol. Chem. (0021-9258) 2001 Self-trimerization of ExsD limits inhibition of the Pseudomonas aeruginosa transcriptional activator ExsA in vitro. Self-trimerization of ExsD limits inhibition of the Pseudomonas aeruginosa transcriptional activator ExsA in vitro. FEBS J. (1742-464X) 2013 Bernhards RC., Marsden AE., Esher SK., Yahr TL., Schubot FD. suggested by lperfetto ecoli Escherichia coli (strain K12) complementation protein complementation assay PCA complementation predetermined predetermined participant predetermined Bernhards RC., Marsden AE., Esher SK., Yahr TL., Schubot FD. suggested by lperfetto FEBS J. (1742-464X) 2013 Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR. Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR. EMBO Rep. (1469-221X) 2010 imex curation Chen H., Yi C., Zhang J., Zhang W., Ge Z., Yang CG., He C. chenhao@nju.edu.cn Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Chen H., Yi C., Zhang J., Zhang W., Ge Z., Yang CG., He C. chenhao@nju.edu.cn EMBO Rep. (1469-221X) 2010 Only protein-protein interactions imex curation An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. FEBS letters 2015 imex curation An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr 03-Dec-2015: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr Accepted 2015-NOV-09 AT 14:19 GMT AT 14:19 GMT by LUANA FEBS letters 2015 Only protein-protein interactions imex curation imex curation apra_pseae Serralysin Alkaline metalloproteinase PA1249 aprA protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSSNSLALKGRSDAYTQVDNFLHAYARGGDELVNGHPSYTVDQAAEQILREQASWQKAPGDSVLTLSYSFLTKPNDFFNTPWKYVSDIYSLGKFSAFSAQQQAQAKLSLQSWSDVTNIHFVDAGQGDQGDLTFGNFSSSVGGAAFAFLPDVPDALKGQSWYLINSSYSANVNPANGNYGRQTLTHEIGHTLGLSHPGDYNAGEGDPTYADATYAEDTRAYSVMSYWEEQNTGQDFKGAYSSAPLLDDIAAIQKLYGANLTTRTGDTVYGFNSNTERDFYSATSSSSKLVFSVWDAGGNDTLDFSGFSQNQKINLNEKALSDVGGLKGNVSIAAGVTVENAIGGSGSDLLIGNDVANVLKGGAGNDILYGGLGADQLWGGAGADTFVYGDIAESSAAAPDTLRDFVSGQDKIDLSGLDAFVNGGLVLQYVDAFAGKAGQAILSYDAASKAGSLAIDFSGDAHADFAINLIGQATQADIVV mint 1865EA8F94232663 q9i157_pseae pvdL PA2424 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MMDAFELPTTLVQALRRRAVQEPERLALRFLAEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASSFFACYGLAEATLFVTGGQRGQGIPALAVDGEALARNRIAEGEGSVLMCCGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVERDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEVPSARKGRVAAFAVTVDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLEDGSLDSYALFPGLQAVQEAQPPAGDDELLARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVVAQVRDSLGVALDLRQLFEAPTLQAFSATVARQLAAGLPAEAPMAHLPRGVDLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFAWQFVDLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQVLAACGQGGQLFQVLFNHQQRDLSALRRLPGLLADELPWHSREAKFDLQLQSEEDARGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIALVDAEQAAHLAEWGSAPCEPARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQREHVEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLATRIVSRTRQACDVELPLRALFEASELEAFCEQVRAAQAAGRTDSHGAIRRIDREQPVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDWQDFSALDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQTRQLAGMTVEYIANDARATKFDLNLEVTDLDQRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQRRIAELPLFAAEERKQLLLAGTAGEAGLQDTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAALFEALGELPAGVARWCLEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYVASAVAEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPAPDPALNRQAYEAPRSVLEQQLAGVWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQSLAAVARHSQASQAEQGPVQGDSALTPIQHWFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLREQELLWHVPVQSFDECAELFAKAQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRDWAGRLQAYAGSESLREELGWWQARLGGQPVEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSTLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAQSPGESIKAIKEQLRAVPHKGLGYGVLRYLADPAVRQAMAALPTAPITFNYLGQFDQSFADALFQPLDQPTGPIHDEQAPLPNELSVDGQVYGGELVLRWTYSRERYDARTVNELAQAYLAELQALIEHCLEDGAGGLTPSDFPLAQLSQAQLDALAVPAGEIEDVYPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGRTRIEFLDWSELPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGESRPANLPTPPRYRDYIAWLQRQDLEQSRRWWSESLRGFERPTLVPSDRPFLREHAGESGGMIVGDRYTRLDAADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPVGMPEMQRTVGLFINSIPLRVQMPAAGQRCTVREWLNRLFERNLELREHEHLPLVAIQESSELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTVVCYPGDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALADGFHGELEALPLLGEDERDFLLDGCNRSARDYPLEQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQACREQALALFDELGCVDRPRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTYLPIGSPTDNNRLYLLGAGADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVPGETPRSSADSPAGLMVEQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIGQMQNQAYQAPRNELEETLARIWAEVLKVERVGVFDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTVEELASYIESLAPSEISEQKAERLNDLMSKLEML 6A559D342ECC1C9A q9hvi8_pseae PA4601 morA protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSTPSLTPSPPPAGDPLTVPDRPAAKAGLLLLVLLMLGLLLWQMSQELRQQERFEHERAAAQLDRLNDRLSLTLELKARTALALLPGVPPSERGEIQGRLLPRISDALPQVRQLQWVDSAPQTDSPSPETTLPEQLRQHAGSGLYHYCLDPRDGESLYLTLREPGSRRDSGFWLLHLASDSLAQWSPDLPTGNLLWRLEDQYAGRVLWHTPGSTALLDDMQTLGVEPLRNSDWQLRGLYDSTRVRLGLLPGIGGELAIFLLLVGVTVYMLLRLHREQQGLRAMTLASQRSLRQAATALAAIDERVLVTRADGRLSYLNPQAERLFGISSAQARQHHLLGLLPDLEPGWLTDAGGDGETRSELLPLRVRGEPRTFTLSRHPLASYPALADQAWTLREQILQGGQVWVLRDVTEEQHALGVLEETRRRYQDIFEGVGVALCVLDLSALRQALVEQGLDSCAALRAWLAGEPGRQQALLERIRITEINDVSRRLLQIDSTEQAWQRLLDHGPLQPDSLRLQVIEALIERRPVLELEATLRCGKSTPRHLWLQLRLPENPGEWHAVTLSLSDVTSRKEVELSLIEREKFWSDAVQAVPDTLYIHDLHARRVIFSNHHLGQQLGYNQEELARMGENFWETLLHPDDQEYYWRIRNLQHVVGDGLLLDSQLRWRHRDGRWHWFDIREQAFSRDRSGRVARLIGVAKDITFTVEANNALRENGRRYRMLAENISDVIFSTDAELNASYVSPSVQHVFGYSPEWALLNGLHQTATNPRQLGRLNGLLRRVRHAIGDRQKLAELRENPGQHLFALDCLRADGRKIPIELRIVLMWDEHDRFEGLLGIARDISQQRRAERELRMAATVFEHSTAAIMVTDPAGYIVQVNDSFSRLTGYSPADVLDQQPRLLTADRQEANQLKHVLASLQHSGSWEGEILQKRKTGELYPSWVGITAVRDEEGDLVSFVCFFSDISERKASERRIHRLAYYDALTHLPNRTLFQDRLHTALQQAERNGQWVVLMFLDLDRFKPINDSLGHAAGDRMLQEVATRLSACVSQDDTVARMGGDEFTLLLPSQGDREIALKRAIQVAELILGRLARPFTLEGREFFVTASIGVALSPQDGAELSLLMKNADTAMYHAKEMGKNNFQFYQAEMNARALERLELESDLRRALELGEFVLHYQPQFTGDGRRLTGAEALLRWQHPRRGLVPPSEFIPVLEEIGLVAQVGDWLLAEACKQLRSWHKAKVRVPKVSVNLSARQFADGQLGERIAAILYETGIPPACLELELTESILMSDVAEAMQILSGLKRLGLAIAVDDFGTGYSSLNYLKQFPIDVLKIDRSFVDGLPHGEQDAQIARAIIAMAHSLNLMVIAEGVESQAQLDFLREHGCDEVQGYLFGRPMPAEQFGMLYASDVLFMFNEG F12347DD0BA889E2 q9hy81_pseae Alkyl hydroperoxide reductase C Peroxiredoxin Thioredoxin peroxidase PA3529 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSVLVGKKAPDFNVAAVLGNGEIVESFTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTHNAWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDVESDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDALQFHEEHGEVCPANWKKGDKGMTASPEGVAKYLAENASKL D42EB998870CA489 mexr_pseae Multidrug resistance operon repressor mexR PA0424 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MNYPVNPDLMPALMAVFQHVRTRIQSELDCQRLDLTPPDVHVLKLIDEQRGLNLQDLGRQMCRDKALITRKIRELEGRNLVRRERNPSDQRSFQLFLTDEGLAIHQHAEAIMSRVHDELFAPLTPVEQATLVHLLDQCLAAQPLEDI 59F5146394BE89DD 59F5146394BE89DD q9i181_pseae pvdJ PA2400 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSFARLPIPQTRQEMDNLPLSYAQERQWFLWQLEPESSAYHIPTALRLRGRLDIASLQRSFAALVERHESLRTRIARMGDEWVQVVSADVSLALEVEVQRGLDEQRLLERVEAEIARPFDLEQGPLLRVTLLEVDADEHVLVMVQHHIVSDGWSMQLMVEELVQLYAAYSQGLDVVLPALPIQYADYALWQRSWMEAGEKERQLAYWTGLLGGEQPVIELPLDHPRQPLRSYRGAQLDLELEPHLALALKQLVQRKGVTMFMLLLASFQALLHRYSGQADIRVGVPIANRNRVETERLIGFFVNTQVLKADINGRMGFDELLAQARQRALEAQAHQDLPFEQLVEALQPERSLGHNPLFQVMFNHQADSRSANQGVQLPGLSLERMEWRSSSVAFDLTLDVHEAEDGIWASFGYATDLFEASTVERLARHWQNLLRGIVAEPGRPVAELPLLLDEERDCLSRAWAENADEGGLPPLVQLQIQEQARLRPQAQALALEGQALSYAELNARANRLAHCLIARGVGPDVLVGIAVERSLDMVVGLLAILKAGGAYVPLDPTYPQDRLRHMLEDSAVGLLLSQEHLLPGLPLHEGLEVLSIDRLERDASVSTDDPVVNLRPENLAYVIYTSGSTGKPKGVAISHAALAQFSRIASGYSALTPEDRILQFATLSFDGFVEQLYPALTRGACVVLRGGDLWDTGELYRQIVEQGVTLADLPTAYWNLFLLDALAEPRRSYGALRQIHIGGEAMPLEGPKLWRQAGMGRVRLLNTYGPTEATVVSSVFDCSAENARVGNASPIGQALPGRTLLVLDEHLGLLPVGPVGELYIASRAGLARAYHDRPGLTAERFLPDPFGEPGSRLYRTGDLARRRGDGVIEYMGRADHQVKIRGFRIELGEVEARLLDLEGIREAAALALDGQLVAYLVAEGGEDETRQPALRERIRTALRASLPDYMVPSHLLFLERMPLSPNGKLDRRALPKPDAGLMQRDHMAPASALEKDVAAIWGELLGVERVGLTDNFFELGGHSLLATRLVSRIRQDLGIEVSLKSLFEQPVLQGFVESLGEKPAEVPPITPVTREQPLPLSYAQERQWFLWQLEPESAAYHIPAALRLRGGLDVVALQRSFERLAQRHESLRTRFRQEGLRTVQVVDADGQLQVSRHNLANVDDASLRAAVEAEMARPFDLRTDALLRISLFEVAPNDHVLVMVQHHIVSDGWSMQLMVEELVQLYAAYSQGREAALPALPIQYPDYAVWQREWMEAGERERQLAYWIGLLGGEQPVLELPFDRPRPAEQSFRGARLEFELGAERARRLKALAQRQGASTFMLLLASFQALLYRYSGQSDIRVGVPVANRNRVETERLIGFFVNTQVLKADIDGQMGFDRLLHQVRQRSLEAQAHQDLPFEQLVEALQPERSLSHSPLFQVLFNYQAERGEHGLPEVAGLSIEEQAWESHTAQFDLVLDTCESESDIWAALVYATDLFDASTAERLVRHWQNLLDAILAMPDARLGELDMLDREEREVIGQLWNRSDSGYPATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDNRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLATQVIGRLRERLHLEVPIKSMFTAETLGEFCHGVETLKAESAPVEDALAKSLEALKRLSADELEKLIS 302AEEFF838CAB3F pvda_pseae L-ornithine N(5)-monooxygenase L-ornithine N(5)-hydroxylase Pyoverdin biosynthesis protein A pvdA pvd-1 L-ornithine N(5)-oxygenase PA2386 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MTQATATAVVHDLIGVGFGPSNIALAIALQERAQAQGALEVLFLDKQGDYRWHGNTLVSQSELQISFLKDLVSLRNPTSPYSFVNYLHKHDRLVDFINLGTFYPCRMEFNDYLRWVASHFQEQSRYGEEVLRIEPMLSAGQVEALRVISRNADGEELVRTTRALVVSPGGTPRIPQVFRALKGDGRVFHHSQYLEHMAKQPCSSGKPMKIAIIGGGQSAAEAFIDLNDSYPSVQADMILRASALKPADDSPFVNEVFAPKFTDLIYSREHAERERLLREYHNTNYSVVDTDLIERIYGVFYRQKVSGIPRHAFRCMTTVERATATAQGIELALRDAGSGELSVETYDAVILATGYERQLHRQLLEPLAEYLGDHEIGRDYRLQTDERCKVAIYAQGFSQASHGLSDTLLSVLPVRAEEISGSLYQHLKPGTAARALHEHALAS 3971A2B223802ACA azur_pseae Azurin azu PA4922 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MLRKLAAVSLLSLLSAPLLAAECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTFPGHSALMKGTLTLK 9C3881D7B6D64B67 mint 9C3881D7B6D64B67 q9i182_pseae pvdD PA2399 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MQALIEKVGSLSPQERKALAVLLKQQGVNLFEIAPVFKRQDGEPLRLSYAQERQWFLWQLEPESAAYHIPSVLRLRGRLDLDALQRSFDSLVARHETLRTRFRLDGDEARQEIAASMALPLDIVALGPLEEGALARQVETTIARPFDLERGPLLRVSLLRLAEDDHVLVLVQHHIVSDGWSMQVMVEELVQLYAAYSRGLEVALPALPIQYADYALWQRSWMEAGEKERQLAYWTGLLGGEQPVLELPFDRPRPVRQSHRGAQFILELDIDLSQALRRVAQQEGATAFALLLASFQALLYRYSGQADIRVGVPIANRNRVETERLIGFFVNTQVLKADLDGRMGFDELLAQARQRALEAQAHQDLPFEQLVEALQPERSLSHNPLFQVLFNYQSEARGNGQAFRFDELQMESVQFDSRTAQFDLTLDLTDEEQRFCAVFDYATDLFDASTVERLAGHWRNLLRGIVANPRQRLGELPLLDAPERRQTLSEWNPAQRECAVQGTLQQRFEEQARQRPQAVALILDEQRLSYGELNARANRLAHCLIARGVGADVPVGLALERSLDMLVGLLAILKAGGAYLPLDPAAPEERLAHILDDSGVRLLLTQGHLLERLPRQAGVEVLAIDGLVLDGYAESDPLPTLSADNLAYVIYTSGSTGKPKGTLLTHRNALRLFSATEAWFGFDERDVWTLFHSYAFDFSVWEIFGALLYGGCLVIVPQWVSRSPEDFYRLLCREGVTVLNQTPSAFKQLMAVACSADMATQQPALRYVIFGGEALDLQSLRPWFQRFGDRQPQLVNMYGITETTVHVTYRPVSEADLEGGLVSPIGGTIPDLSWYILDRDLNPVPRGAVGELYIGRAGLARGYLRRPGLSATRFVPNPFPGGAGERLYRTGDLARFQADGNIEYIGRIDHQVKVRGFRIELGEIEAALAGLAGVRDAVVLAHDGVGGTQLVGYVVADSAEDAERLRESLRESLKRHLPDYMVPAHLMLLERMPLTVNGKLDRQALPQPDASLSQQAYRAPGSELEQRIAAIWSEILGVERVGLDDNFFELGGHSLLATRVISRVRQEQQLDASLKALFERPVLEAFAQGLERTTDAVSTIPLADRQQPLALSFAQERQWFLWQLEPESAAYHIPSALRLRGRLDVDALQRSFDSLVARHETLRTRFRLEGGRSYQQVQPAVSVSIEREQFGEEGLIERIQAIVVQPFDLERGPLLRVNLLQLAEDDHVLVLVQHHIVSDGWSMQVMVEELVQLYAAYSQGLDVVLPALPIQYADYALWQRSWMEAGEKERQLAYWTGLLGGEQPVLELPFDRPRPARQSHRGAQLGFELSRELVEAVRALAQREGASSFMLLLASFQALLYRYSGQADIRVGVPIANRNRVETERLIGFFVNTQVLKADLDGRMGFDELLAQARQRALEAQAHQDLPFEQLVEALQPERNASHNPLFQVLFNHQSEIRSVTPEVQLEDLRLEGLAWDGQTAQFDLTLDIQEDENGIWASFDYATDLFDASTVERLAGHWRNLLRGIVANPRQRLGELPLLDAPERRQTLSEWNPAQRECAVQGTLQQRFEEQARQRPQAVALILDEQRLSYGELNARANRLAHCLIARGVGADVPVGLALERSLDMLVGLLAILKAGGAYLPLDPAAPEERLAHILDDSGVRLLLTQGHLLERLPRQAGVEVLAIDGLVLDGYAESDPLPTLSADNLAYVIYTSGSTGKPKGTLLTHRNALRLFSATEAWFGFDERDVWTLFHSYAFDFSVWEIFGALLYGGRLVIVPQWVSRSPEDFYRLLCREGVTVLNQTPSAFKQLMAVACSADMATQQPALRYVIFGGEALDLQSLRPWFQRFGDRQPQLVNMYGITETTVHVTYRPVSEADLKGGLVSPIGGTIPDLSWYILDRDLNPVPRGAVGELYIGRAGLARGYLRRPGLSATRFVPNPFPGGAGERLYRTGDLARFQADGNIEYIGRIDHQVKVRGFRIELGEIEAALAGLAGVRDAVVLAHDGVGGTQLVGYVVADSAEDAERLRESLRESLKRHLPDYMVPAHLMLLERMPLTVNGKLDRQALPQPDASLSQQAYRAPGSELEQRIAAIWAEILGVERVGLDDNFFELGGHSLLLLMLKERIGDTCQATLSISQLMTHASVAEQAACIEGQARESLLVPLNGRREGSPLFMFHPSFGSVHCYKTLAMALRDRHPVKGVVCRALLGAGREVPEWDDMVAEYAEQLLQEHPEGVFNLAGWSLGGNLAMDVAARLEQRGRQVAFVGWIDAPAPVRVEAFWNEIGPTPEAVPNLSVGEMRVELLGVMFPERAEHIERAWSSICSATTDDEQRWTRMSDWAEAEIGAEFATLRSEIAQSNELEVSWELKQILDERLKAMDYPRLTAKVSLWWAARSTNAIQRSAVERSMAEAIGAERVEPVRVLDTRHDKIIDHPEFVQSFRAALERAGR 62EC4A9BAB1BAAA4 q9i5i9_pseae sdsA1 PA0740 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSRLLALLALAPLLAGAAETTAPKPPSAFTVEAQRRVEAELPFADRADFERADRGLIRRPERLLIRNPDGSVAWQLGGYDFLLDGKPRDSINPSLQRQALLNLKYGLFEVAEGIYQVRGFDLANITFIRGDSGWIVVDTLTTPATARAAYELVSRELGERPIRTVIYSHAHADHFGGVRGLVEPQQVASGAVQIIAPAGFMEAAIKENVLAGNAMMRRATYQYGTQLPKGPQGQVDMAIGKGLARGPLSLLAPTRLIEGEGEDLVLDGVPFTFQNTPGTESPAEMNIWLPRQKALLMAENVVGTLHNLYTLRGAEVRDALGWSKYINQALHRFGRQAEVMFAVHNWPRWGNAEIVEVLEKQRDLYGYLHDQTLHLANQGVTIGQVHNRLRLPPSLDQEWYDRGYHGSVSHNARAVLNRYLGYYDGNPATLDPLSPEDSAGRYVEYMGGAERLLEQARASYARGEYRWVVEVVNRLVFAEPDNRAARELQADALEQLGYQAENAGWRNSYLSAAYELRHGVPRDQPTMKAGSADALAAMDTGLLFDYLGVRLDAGAAEGKALSINLRLPDIGENYLLELKNSHLNNLRGVQSEDAGQTVSIDRADLNRLLLKEVSAVRLVFEGKLKSSGNPLLLGQLFGMLGDFDFWFDIVTPAAKSEG DIP protein Q9I5I9 original sequence version: 85 3D29B5D2B0A2A84F inh_pseae Proteinase inhibitor inh aprI PA1250 Aprin protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSASAKLSRMVCLLCGFFSTGISMASSLILLSASDLAGQWTLQQDEAPAICHLELRDSEVAEASGYDLGGDTACLTRWLPSEPRAWRPTPAGIALLERGGLTLMLLGRQGEGDYRVQKGDGGQLVLRRATP mint Inhibitor of the alkaline protease. It forms a non-covalent bond with the protease and may prevent its autocatalytic cleavage in the periplasm 8CE4A64ED10AA8CD rp54_pseae RNA polymerase sigma-54 factor rpoN PA4462 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MKPSLVLKMGQQLTMTPQLQQAIRLLQLSTLDLQQEIQEALESNPMLERQEDGDDFDNSDPLADGAEQAASAPQESPLQESATPSVESLDDDQWSERIPSELPVDTAWEDIYQTSASSLPSNDDDEWDFTARTSSGESLHSHLLWQVNLAPMSDTDRMIAVTIIDSINNDGYLEESLEEILAAIDPELDVELDEVEVVLRRIQQLEPAGIGARNLRECLLLQLRQLPSTTPWLNEALRLVSDYLDLLGGRDYSQLMRRMKLKEDELRQVIELIQCLHPRPGSQIESSEAEYIVPDVIVRKDNERWLVELNQEAMPRLRVNATYAGMVRRADSSADNTFMRNQLQEARWFIKSLQSRNETLMKVATQIVEHQRGFLDYGEEAMKPLVLHDIAEAVGMHESTISRVTTQKYMHTPRGIFELKYFFSSHVSTAEGGECSSTAIRAIIKKLVAAENAKKPLSDSKIAGLLEAQGIQVARRTVAKYRESLGIAPSSERKRLV mint CE1994F03FD58405 exsa_pseae HTH-type transcriptional regulator ExsA exsA PA1713 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MQGAKSLGRKQITSCHWNIPTFEYRVNKEEGVYVLLEGELTVQDIDSTFCLAPGELLFVRRGSYVVSTKGKDSRILWIPLSAQFLQGFVQRFGALLSEVERCDEPVPGIIAFAATPLLAGCVKGLKELLVHEHPPMLACLKIEELLMLFAFSPQGPLLMSVLRQLSNRHVERLQLFMEKHYLNEWKLSDFSREFGMGLTTFKELFGSVYGVSPRAWISERRILYAHQLLLNSDMSIVDIAMEAGFSSQSYFTQSYRRRFGCTPSRSRQGKDECRAKNN 4823D0E9135E0BB7 apra-inh 15 19 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 29 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 direct interaction direct interaction In the xray complex 1jiw, Q03026 is chain I and Q03023 is chain P Resolution 1.740 mint mexr 10 MexR 23 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 2.0 direct interaction direct interaction mint Coordinates and structure factors heve been deposited in the Protein Data Bank with accession code 3MEX. f2b f2c f2d f3 f4 st1 sf2 sf4 sf5 mexr-1 17 MexR 23 weight by comassie molecular weight estimation by coomasie staining weight by comassie predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 2.0 direct interaction direct interaction sf1b mint exsa-exsa-2 16 ExsA 31 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ExsA 31 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association f4 mint Using a bacterial mono-hybrid assay, we were able to demonstrate that ExsDM59R expression efficiently disrupts ExsA dimerization (Fig. 4) rpon-rpon-2 14 P. aeruginosa σ54 30 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P. aeruginosa σ54 30 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association f2c mint P. aeruginosa As shown in Fig. 2C, P. aeruginosa σ54/σ54 interaction resulted as strong as for P. putida, suggesting that this feature might be conserved in the Pseudomonas genus. On the contrary, E. coli σ54/σ54 interaction was undetectable in this assay. azu 5 Azurin 26 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 12.0 direct interaction direct interaction mint t1 sf sf3 Coordinates have been deposited with the Protein Data Bank (PDB-ID 3N2J). pvda-pvdd 7 PvdA 25 unspecified role unspecified role bait bait purified purified tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined PvdL 20 unspecified role unspecified role prey prey cell lysate cell lysate PvdJ 24 unspecified role unspecified role prey prey cell lysate cell lysate association association f3a pvda-pvdj-1 11 PvdA 25 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed tag fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined PvdJ 24 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed tag fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association f3b pvda-pvdj-2 1 PvdA 25 unspecified role unspecified role unspecified role unspecified role living cell living cell tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range PvdJ 24 unspecified role unspecified role unspecified role unspecified role living cell living cell tag eyfp enhanced yellow fluorescent protein tag eyfp n-term range n-terminal range n-term range n-term range n-terminal range n-term range colocalization colocalization f4 sf3 Iron-depleted P. aeruginosa cells were analyzed by confocal laser scanning microscopy to assess the in vivo localization of ECFP- and EYFP-tagged proteins. The two protein pairs (PvdA-ECFP/EYFP-PvdJ and PvdA-ECFP/PvdD-EYFP) clearly co-localized in both exponential and stationary phase cells (Figs. 4 and S3). During early exponential phase, this protein complex was mainly detected at cell poles (Fig. 4). Such polar localization was less evident in late exponential and stationary phase cells, where proteins appeared more homogeneously distributed at the cell periphery (Fig. S3). pvda-pvdd-1 1 PvdD 27 unspecified role unspecified role unspecified role unspecified role living cell living cell tag eyfp enhanced yellow fluorescent protein tag eyfp c-term range C-terminal range c-term range c-term range C-terminal range c-term range PvdA 25 unspecified role unspecified role unspecified role unspecified role living cell living cell tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range colocalization colocalization f4 sf3 Iron-depleted P. aeruginosa cells were analyzed by confocal laser scanning microscopy to assess the in vivo localization of ECFP- and EYFP-tagged proteins. The two protein pairs (PvdA-ECFP/EYFP-PvdJ and PvdA-ECFP/PvdD-EYFP) clearly co-localized in both exponential and stationary phase cells (Figs. 4 and S3). During early exponential phase, this protein complex was mainly detected at cell poles (Fig. 4). Such polar localization was less evident in late exponential and stationary phase cells, where proteins appeared more homogeneously distributed at the cell periphery (Fig. S3). mora 8 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction t1 f2 mora-1 8 21 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain true direct interaction direct interaction t1 f3 q88nw9_psepk-1 9 22 unspecified role unspecified role neutral component neutral component purified purified 22 unspecified role unspecified role neutral component neutral component purified purified Q9HY81:p.Ala112Cys mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain A C Wed May 02 17:44:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala112cys' Tue Jun 30 18:11:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala112Cys' direct interaction direct interaction f1 sf2 f2d F-1 (HMW protein complexes) and F-2 (LMW forms) fractions displayed opposite pattern in peroxidase and chaperone activities. The F-1 fraction exhibited high chaperone activity and low peroxidase activity, whereas the F-2 fraction displayed high peroxidase activity with low chaperone activity (Fig. 1B). These results suggested that oligomerization of the protein into HMW complexes promotes chaperone activity while dissociation of the HMW complexes into LMW species enhances peroxidase activity. q9hy81_pseae-q9hy81_pseae-1 4 22 unspecified role unspecified role neutral component neutral component purified purified 22 unspecified role unspecified role neutral component neutral component purified purified Q9HY81:p.Ala112Cys mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain A C Wed May 02 18:41:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala112cys' Tue Jun 30 19:52:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala112Cys' direct interaction direct interaction f2a f2b q9hy81_pseae-q9hy81_pseae-2 18 22 unspecified role unspecified role neutral component neutral component purified purified 22 unspecified role unspecified role neutral component neutral component purified purified Q9HY81:p.Ala112Cys mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain A C Wed May 02 20:32:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala112cys' Tue Jun 30 17:43:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala112Cys' direct interaction direct interaction f3 sdsa1-1 2 28 unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f3 sf6 f6d sdsa1-2 12 28 unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction sf2 sf3 f6 f7 sdsa1-3 3 28 unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f4 sdsa1-5 6 28 unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f8 sdsa1-4 13 28 unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f9 f6a f6b f6c f4 DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wilke MS., Heller M., Creagh AL., Haynes CA., McIntosh LP., Poole K., Strynadka NC. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Wilke MS., Heller M., Creagh AL., Haynes CA., McIntosh LP., Poole K., Strynadka NC. DIP original experiment: DIP-113411X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wilke MS., Heller M., Creagh AL., Haynes CA., McIntosh LP., Poole K., Strynadka NC. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Wilke MS., Heller M., Creagh AL., Haynes CA., McIntosh LP., Poole K., Strynadka NC. DIP original experiment: DIP-113413X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wilke MS., Heller M., Creagh AL., Haynes CA., McIntosh LP., Poole K., Strynadka NC. Only protein-protein interactions in vitro In vitro comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel predetermined predetermined participant predetermined Wilke MS., Heller M., Creagh AL., Haynes CA., McIntosh LP., Poole K., Strynadka NC. DIP original experiment: DIP-113414X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. Nature 2011 imex curation Huang CS., Ge P., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Huang CS., Ge P., Zhou ZH., Tong L. DIP original experiment: DIP-249464X Nature 2011 IMEx An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structure (London, England : 1993) 2009 imex curation Navarro MV., De N., Bae N., Wang Q., Sondermann H. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Navarro MV., De N., Bae N., Wang Q., Sondermann H. DIP original experiment: DIP-132027X Structure (London, England : 1993) 2009 IMEx Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. MgATP regulates allostery and fiber formation in IMPDHs. MgATP regulates allostery and fiber formation in IMPDHs. Structure (London, England : 1993) 2013 imex curation Labesse G., Alexandre T., Vaupré L., Salard-Arnaud I., Him JL., Raynal B., Bron P., Munier-Lehmann H. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Labesse G., Alexandre T., Vaupré L., Salard-Arnaud I., Him JL., Raynal B., Bron P., Munier-Lehmann H. DIP original experiment: DIP-252310X Structure (London, England : 1993) 2013 IMEx MgATP regulates allostery and fiber formation in IMPDHs. The Structure of the Toxin and Type Six Secretion System Substrate Tse2 in Complex with Its Immunity Protein. The Structure of the Toxin and Type Six Secretion System Substrate Tse2 in Complex with Its Immunity Protein. Structure (London, England : 1993) 2016 imex curation Robb CS., Robb M., Nano FE., Boraston AB. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Robb CS., Robb M., Nano FE., Boraston AB. DIP original experiment: DIP-268438X Structure (London, England : 1993) 2016 IMEx The Structure of the Toxin and Type Six Secretion System Substrate Tse2 in Complex with Its Immunity Protein. HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. PLoS biology 2012 imex curation Airola MV., Sukomon N., Samanta D., Borbat PP., Freed JH., Watts KJ., Crane BR. Only protein-protein interactions ecolx Escherichia coli epr electron paramagnetic resonance ESR EPR EPR ESR epr predetermined predetermined participant predetermined Airola MV., Sukomon N., Samanta D., Borbat PP., Freed JH., Watts KJ., Crane BR. DIP original experiment: DIP-252408X PLoS biology 2012 IMEx HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. PLoS biology 2012 imex curation Airola MV., Sukomon N., Samanta D., Borbat PP., Freed JH., Watts KJ., Crane BR. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Airola MV., Sukomon N., Samanta D., Borbat PP., Freed JH., Watts KJ., Crane BR. DIP original experiment: DIP-252406X PLoS biology 2012 IMEx HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature 2011 imex curation Zhao Y., Yang J., Shi J., Gong YN., Lu Q., Xu H., Liu L., Shao F. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Zhao Y., Yang J., Shi J., Gong YN., Lu Q., Xu H., Liu L., Shao F. DIP original experiment: DIP-218900X Nature 2011 IMEx The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Conformational differences between the Pfr and Pr states in Pseudomonas aeruginosa bacteriophytochrome. Conformational differences between the Pfr and Pr states in Pseudomonas aeruginosa bacteriophytochrome. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Yang X., Kuk J., Moffat K. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Yang X., Kuk J., Moffat K. DIP original experiment: DIP-134499X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Conformational differences between the Pfr and Pr states in Pseudomonas aeruginosa bacteriophytochrome. The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wilke MS., Heller M., Creagh AL., Haynes CA., McIntosh LP., Poole K., Strynadka NC. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Wilke MS., Heller M., Creagh AL., Haynes CA., McIntosh LP., Poole K., Strynadka NC. DIP original experiment: DIP-113412X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria. Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Nocek B., Kochinyan S., Proudfoot M., Brown G., Evdokimova E., Osipiuk J., Edwards AM., Savchenko A., Joachimiak A., Yakunin AF. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Nocek B., Kochinyan S., Proudfoot M., Brown G., Evdokimova E., Osipiuk J., Edwards AM., Savchenko A., Joachimiak A., Yakunin AF. DIP original experiment: DIP-133449X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria. The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket. The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Bokhove M., Nadal Jimenez P., Quax WJ., Dijkstra BW. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Bokhove M., Nadal Jimenez P., Quax WJ., Dijkstra BW. DIP original experiment: DIP-215895X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket. Structural basis for the transcriptional regulation of membrane lipid homeostasis. Structural basis for the transcriptional regulation of membrane lipid homeostasis. Nature structural & molecular biology 2010 imex curation Miller DJ., Zhang YM., Subramanian C., Rock CO., White SW. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Miller DJ., Zhang YM., Subramanian C., Rock CO., White SW. DIP original experiment: DIP-217577X Nature structural & molecular biology 2010 IMEx Structural basis for the transcriptional regulation of membrane lipid homeostasis. The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases. The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Hagelueken G., Adams TM., Wiehlmann L., Widow U., Kolmar H., Tümmler B., Heinz DW., Schubert WD. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Hagelueken G., Adams TM., Wiehlmann L., Widow U., Kolmar H., Tümmler B., Heinz DW., Schubert WD. DIP original experiment: DIP-262920X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases. An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. Nature 2011 imex curation Huang CS., Ge P., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Huang CS., Ge P., Zhou ZH., Tong L. DIP original experiment: DIP-249467X Nature 2011 IMEx An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. MgATP regulates allostery and fiber formation in IMPDHs. MgATP regulates allostery and fiber formation in IMPDHs. Structure (London, England : 1993) 2013 imex curation Labesse G., Alexandre T., Vaupré L., Salard-Arnaud I., Him JL., Raynal B., Bron P., Munier-Lehmann H. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Labesse G., Alexandre T., Vaupré L., Salard-Arnaud I., Him JL., Raynal B., Bron P., Munier-Lehmann H. DIP original experiment: DIP-252311X Structure (London, England : 1993) 2013 IMEx MgATP regulates allostery and fiber formation in IMPDHs. Crystal structure of RNase T, an exoribonuclease involved in tRNA maturation and end turnover. Crystal structure of RNase T, an exoribonuclease involved in tRNA maturation and end turnover. Structure (London, England : 1993) 2007 imex curation Zuo Y., Zheng H., Wang Y., Chruszcz M., Cymborowski M., Skarina T., Savchenko A., Malhotra A., Minor W. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Zuo Y., Zheng H., Wang Y., Chruszcz M., Cymborowski M., Skarina T., Savchenko A., Malhotra A., Minor W. DIP original experiment: DIP-66880X Structure (London, England : 1993) 2007 IMEx Crystal structure of RNase T, an exoribonuclease involved in tRNA maturation and end turnover. Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG. Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG. Nature structural & molecular biology 2017 imex curation Luo Q., Yang X., Yu S., Shi H., Wang K., Xiao L., Zhu G., Sun C., Li T., Li D., Zhang X., Zhou M., Huang Y. yihuahuang@sun5.ibp.ac.cn 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation ecoli Escherichia coli (strain K12) x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction structure determination identification by structure determination identification by structure determination structure determination Luo Q., Yang X., Yu S., Shi H., Wang K., Xiao L., Zhu G., Sun C., Li T., Li D., Zhang X., Zhou M., Huang Y. yihuahuang@sun5.ibp.ac.cn Accepted 2019-APR-30 AT 10:08 BST AT 10:08 BST by ORCHARD Nature structural & molecular biology 2017 imex curation From the first paragraph in the method section, it seemed as if the His tag is only on lptB. The paragraph related to figure 2 is about investigating the effect of His tag on lptB on the complex activity. Therefore, it is unlikely that the His tag was present on other proteins. It looks as if the figure legend was not accurate. Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome. Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome. Nature 2011 imex curation Yang X., Ren Z., Kuk J., Moffat K. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Yang X., Ren Z., Kuk J., Moffat K. DIP original experiment: DIP-248976X Nature 2011 IMEx Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome. MgATP regulates allostery and fiber formation in IMPDHs. MgATP regulates allostery and fiber formation in IMPDHs. Structure (London, England : 1993) 2013 imex curation Labesse G., Alexandre T., Vaupré L., Salard-Arnaud I., Him JL., Raynal B., Bron P., Munier-Lehmann H. Only protein-protein interactions ecolx Escherichia coli 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Labesse G., Alexandre T., Vaupré L., Salard-Arnaud I., Him JL., Raynal B., Bron P., Munier-Lehmann H. DIP original experiment: DIP-252314X Structure (London, England : 1993) 2013 IMEx MgATP regulates allostery and fiber formation in IMPDHs. Structure of concatenated HAMP domains provides a mechanism for signal transduction. Structure of concatenated HAMP domains provides a mechanism for signal transduction. Structure (London, England : 1993) 2010 imex curation Airola MV., Watts KJ., Bilwes AM., Crane BR. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Airola MV., Watts KJ., Bilwes AM., Crane BR. DIP original experiment: DIP-216854X Structure (London, England : 1993) 2010 IMEx Structure of concatenated HAMP domains provides a mechanism for signal transduction. Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Hagelueken G., Wiehlmann L., Adams TM., Kolmar H., Heinz DW., Tümmler B., Schubert WD. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Hagelueken G., Wiehlmann L., Adams TM., Kolmar H., Heinz DW., Tümmler B., Schubert WD. DIP original experiment: DIP-114002X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. In vitro self-assembly of tailorable nanotubes from a simple protein building block. In vitro self-assembly of tailorable nanotubes from a simple protein building block. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Ballister ER., Lai AH., Zuckermann RN., Cheng Y., Mougous JD. Only protein-protein interactions ecolx Escherichia coli comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Ballister ER., Lai AH., Zuckermann RN., Cheng Y., Mougous JD. DIP original experiment: DIP-68501X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx In vitro self-assembly of tailorable nanotubes from a simple protein building block. HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. PLoS biology 2012 imex curation Airola MV., Sukomon N., Samanta D., Borbat PP., Freed JH., Watts KJ., Crane BR. Only protein-protein interactions ecolx Escherichia coli epr electron paramagnetic resonance ESR EPR EPR ESR epr predetermined predetermined participant predetermined Airola MV., Sukomon N., Samanta D., Borbat PP., Freed JH., Watts KJ., Crane BR. DIP original experiment: DIP-252407X PLoS biology 2012 IMEx HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket. The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Bokhove M., Nadal Jimenez P., Quax WJ., Dijkstra BW. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Bokhove M., Nadal Jimenez P., Quax WJ., Dijkstra BW. DIP original experiment: DIP-215896X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket. Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria. Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Nocek B., Kochinyan S., Proudfoot M., Brown G., Evdokimova E., Osipiuk J., Edwards AM., Savchenko A., Joachimiak A., Yakunin AF. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Nocek B., Kochinyan S., Proudfoot M., Brown G., Evdokimova E., Osipiuk J., Edwards AM., Savchenko A., Joachimiak A., Yakunin AF. DIP original experiment: DIP-133451X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria. Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structure (London, England : 1993) 2009 imex curation Navarro MV., De N., Bae N., Wang Q., Sondermann H. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Navarro MV., De N., Bae N., Wang Q., Sondermann H. DIP original experiment: DIP-132026X Structure (London, England : 1993) 2009 IMEx Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Leiman PG., Basler M., Ramagopal UA., Bonanno JB., Sauder JM., Pukatzki S., Burley SK., Almo SC., Mekalanos JJ. Only protein-protein interactions ecolx Escherichia coli 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Leiman PG., Basler M., Ramagopal UA., Bonanno JB., Sauder JM., Pukatzki S., Burley SK., Almo SC., Mekalanos JJ. DIP original experiment: DIP-133829X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket. The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Bokhove M., Nadal Jimenez P., Quax WJ., Dijkstra BW. Only protein-protein interactions ecolx Escherichia coli dls dynamic light scattering dls predetermined predetermined participant predetermined Bokhove M., Nadal Jimenez P., Quax WJ., Dijkstra BW. DIP original experiment: DIP-215897X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket. An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane. An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane. Nature structural & molecular biology 2007 imex curation Moraes TF., Bains M., Hancock RE., Strynadka NC. Only protein-protein interactions pseai Pseudomonas aeruginosa x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Moraes TF., Bains M., Hancock RE., Strynadka NC. DIP original experiment: DIP-66611X Nature structural & molecular biology 2007 IMEx An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane. Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Hagelueken G., Wiehlmann L., Adams TM., Kolmar H., Heinz DW., Tümmler B., Schubert WD. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Hagelueken G., Wiehlmann L., Adams TM., Kolmar H., Heinz DW., Tümmler B., Schubert WD. DIP original experiment: DIP-114000X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. In vitro self-assembly of tailorable nanotubes from a simple protein building block. In vitro self-assembly of tailorable nanotubes from a simple protein building block. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Ballister ER., Lai AH., Zuckermann RN., Cheng Y., Mougous JD. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Ballister ER., Lai AH., Zuckermann RN., Cheng Y., Mougous JD. DIP original experiment: DIP-68500X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx In vitro self-assembly of tailorable nanotubes from a simple protein building block. The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wilke MS., Heller M., Creagh AL., Haynes CA., McIntosh LP., Poole K., Strynadka NC. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Wilke MS., Heller M., Creagh AL., Haynes CA., McIntosh LP., Poole K., Strynadka NC. DIP original experiment: DIP-113410X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR. Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria. Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Abergel C., Monchois V., Byrne D., Chenivesse S., Lembo F., Lazzaroni JC., Claverie JM. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Abergel C., Monchois V., Byrne D., Chenivesse S., Lembo F., Lazzaroni JC., Claverie JM. DIP original experiment: DIP-261341X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria. Phosphorylation-independent regulation of the diguanylate cyclase WspR. Phosphorylation-independent regulation of the diguanylate cyclase WspR. PLoS biology 2008 imex curation De N., Pirruccello M., Krasteva PV., Bae N., Raghavan RV., Sondermann H. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined De N., Pirruccello M., Krasteva PV., Bae N., Raghavan RV., Sondermann H. DIP original experiment: DIP-68379X PLoS biology 2008 IMEx Phosphorylation-independent regulation of the diguanylate cyclase WspR. UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis. UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis. Nature 2015 imex curation White MD., Payne KA., Fisher K., Marshall SA., Parker D., Rattray NJ., Trivedi DK., Goodacre R., Rigby SE., Scrutton NS., Hay S., Leys D. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined White MD., Payne KA., Fisher K., Marshall SA., Parker D., Rattray NJ., Trivedi DK., Goodacre R., Rigby SE., Scrutton NS., Hay S., Leys D. DIP original experiment: DIP-265924X Nature 2015 IMEx UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis. The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases. The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Hagelueken G., Adams TM., Wiehlmann L., Widow U., Kolmar H., Tümmler B., Heinz DW., Schubert WD. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Hagelueken G., Adams TM., Wiehlmann L., Widow U., Kolmar H., Tümmler B., Heinz DW., Schubert WD. DIP original experiment: DIP-262921X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases. Structural insight into OprD substrate specificity. Structural insight into OprD substrate specificity. Nature structural & molecular biology 2007 imex curation Biswas S., Mohammad MM., Patel DR., Movileanu L., van den Berg B. Only protein-protein interactions ecolx Escherichia coli bn-page blue native page bn-page weight by staining molecular weight estimation by staining weight by staining Biswas S., Mohammad MM., Patel DR., Movileanu L., van den Berg B. DIP original experiment: DIP-68115X Nature structural & molecular biology 2007 IMEx Structural insight into OprD substrate specificity. Phosphorylation-independent regulation of the diguanylate cyclase WspR. Phosphorylation-independent regulation of the diguanylate cyclase WspR. PLoS biology 2008 imex curation De N., Pirruccello M., Krasteva PV., Bae N., Raghavan RV., Sondermann H. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined De N., Pirruccello M., Krasteva PV., Bae N., Raghavan RV., Sondermann H. DIP original experiment: DIP-68377X PLoS biology 2008 IMEx Phosphorylation-independent regulation of the diguanylate cyclase WspR. Structure of concatenated HAMP domains provides a mechanism for signal transduction. Structure of concatenated HAMP domains provides a mechanism for signal transduction. Structure (London, England : 1993) 2010 imex curation Airola MV., Watts KJ., Bilwes AM., Crane BR. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Airola MV., Watts KJ., Bilwes AM., Crane BR. DIP original experiment: DIP-216853X Structure (London, England : 1993) 2010 IMEx Structure of concatenated HAMP domains provides a mechanism for signal transduction. Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Hagelueken G., Wiehlmann L., Adams TM., Kolmar H., Heinz DW., Tümmler B., Schubert WD. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Hagelueken G., Wiehlmann L., Adams TM., Kolmar H., Heinz DW., Tümmler B., Schubert WD. DIP original experiment: DIP-114001X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. Evolutionary origins of the multienzyme architecture of giant fungal fatty acid synthase. Evolutionary origins of the multienzyme architecture of giant fungal fatty acid synthase. Structure (London, England : 1993) 2014 imex curation Bukhari HS., Jakob RP., Maier T. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Bukhari HS., Jakob RP., Maier T. DIP original experiment: DIP-264342X Structure (London, England : 1993) 2014 IMEx Evolutionary origins of the multienzyme architecture of giant fungal fatty acid synthase. An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. Nature 2011 imex curation Huang CS., Ge P., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Huang CS., Ge P., Zhou ZH., Tong L. DIP original experiment: DIP-249465X Nature 2011 IMEx An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. In vitro self-assembly of tailorable nanotubes from a simple protein building block. In vitro self-assembly of tailorable nanotubes from a simple protein building block. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Ballister ER., Lai AH., Zuckermann RN., Cheng Y., Mougous JD. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Ballister ER., Lai AH., Zuckermann RN., Cheng Y., Mougous JD. DIP original experiment: DIP-68499X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx In vitro self-assembly of tailorable nanotubes from a simple protein building block. Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins. Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins. Structure (London, England : 1993) 2014 imex curation Guilvout I., Chami M., Disconzi E., Bayan N., Pugsley AP., Huysmans GH. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Guilvout I., Chami M., Disconzi E., Bayan N., Pugsley AP., Huysmans GH. DIP original experiment: DIP-260620X Structure (London, England : 1993) 2014 IMEx Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins. Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG. Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG. Nature structural & molecular biology 2017 imex curation Luo Q., Yang X., Yu S., Shi H., Wang K., Xiao L., Zhu G., Sun C., Li T., Li D., Zhang X., Zhou M., Huang Y. yihuahuang@sun5.ibp.ac.cn 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation ecoli Escherichia coli (strain K12) pull down pull down predetermined predetermined participant predetermined Luo Q., Yang X., Yu S., Shi H., Wang K., Xiao L., Zhu G., Sun C., Li T., Li D., Zhang X., Zhou M., Huang Y. From the first paragraph in the method section, it seemed as if the His tag is only on lptB. The paragraph related to figure 2 is about investigating the effect of His tag on lptB on the complex activity. Therefore, it is unlikely that the His tag was present on other proteins. It looks as if the figure legend was not accurate. yihuahuang@sun5.ibp.ac.cn Accepted 2019-APR-30 AT 10:08 BST AT 10:08 BST by ORCHARD Nature structural & molecular biology 2017 imex curation From the first paragraph in the method section, it seemed as if the His tag is only on lptB. The paragraph related to figure 2 is about investigating the effect of His tag on lptB on the complex activity. Therefore, it is unlikely that the His tag was present on other proteins. It looks as if the figure legend was not accurate. Metal-binding loop length and not sequence dictates structure. Metal-binding loop length and not sequence dictates structure. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Sato K., Li C., Salard I., Thompson AJ., Banfield MJ., Dennison C. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Sato K., Li C., Salard I., Thompson AJ., Banfield MJ., Dennison C. DIP original experiment: DIP-134041X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Metal-binding loop length and not sequence dictates structure. Structure of the heterotrimeric complex that regulates type III secretion needle formation. Structure of the heterotrimeric complex that regulates type III secretion needle formation. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Quinaud M., Plé S., Job V., Contreras-Martel C., Simorre JP., Attree I., Dessen A. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Quinaud M., Plé S., Job V., Contreras-Martel C., Simorre JP., Attree I., Dessen A. DIP original experiment: DIP-261446X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Structure of the heterotrimeric complex that regulates type III secretion needle formation. Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel. Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel. Structure (London, England : 1993) 2010 imex curation Phan G., Benabdelhak H., Lascombe MB., Benas P., Rety S., Picard M., Ducruix A., Etchebest C., Broutin I. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Phan G., Benabdelhak H., Lascombe MB., Benas P., Rety S., Picard M., Ducruix A., Etchebest C., Broutin I. DIP original experiment: DIP-216856X Structure (London, England : 1993) 2010 IMEx Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel. Structure of the heterotrimeric complex that regulates type III secretion needle formation. Structure of the heterotrimeric complex that regulates type III secretion needle formation. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Quinaud M., Plé S., Job V., Contreras-Martel C., Simorre JP., Attree I., Dessen A. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Quinaud M., Plé S., Job V., Contreras-Martel C., Simorre JP., Attree I., Dessen A. DIP original experiment: DIP-261445X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Structure of the heterotrimeric complex that regulates type III secretion needle formation. Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction. Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Yang X., Kuk J., Moffat K. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Yang X., Kuk J., Moffat K. DIP original experiment: DIP-111299X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction. An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. Nature 2011 imex curation Huang CS., Ge P., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Huang CS., Ge P., Zhou ZH., Tong L. DIP original experiment: DIP-249463X Nature 2011 IMEx An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. MgATP regulates allostery and fiber formation in IMPDHs. MgATP regulates allostery and fiber formation in IMPDHs. Structure (London, England : 1993) 2013 imex curation Labesse G., Alexandre T., Vaupré L., Salard-Arnaud I., Him JL., Raynal B., Bron P., Munier-Lehmann H. Only protein-protein interactions ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined Labesse G., Alexandre T., Vaupré L., Salard-Arnaud I., Him JL., Raynal B., Bron P., Munier-Lehmann H. DIP original experiment: DIP-252312X Structure (London, England : 1993) 2013 IMEx MgATP regulates allostery and fiber formation in IMPDHs. Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins. Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins. Structure (London, England : 1993) 2014 imex curation Guilvout I., Chami M., Disconzi E., Bayan N., Pugsley AP., Huysmans GH. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds western blot western blot Immuno blot Immuno blot Guilvout I., Chami M., Disconzi E., Bayan N., Pugsley AP., Huysmans GH. DIP original experiment: DIP-260619X Structure (London, England : 1993) 2014 IMEx Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins. Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structure (London, England : 1993) 2009 imex curation Navarro MV., De N., Bae N., Wang Q., Sondermann H. Only protein-protein interactions ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined Navarro MV., De N., Bae N., Wang Q., Sondermann H. DIP original experiment: DIP-132028X Structure (London, England : 1993) 2009 IMEx Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome. Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome. Nature 2011 imex curation Yang X., Ren Z., Kuk J., Moffat K. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Yang X., Ren Z., Kuk J., Moffat K. DIP original experiment: DIP-248975X Nature 2011 IMEx Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome. Structural basis for the inhibition of bacterial multidrug exporters. Structural basis for the inhibition of bacterial multidrug exporters. Nature 2013 imex curation Nakashima R., Sakurai K., Yamasaki S., Hayashi K., Nagata C., Hoshino K., Onodera Y., Nishino K., Yamaguchi A. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Nakashima R., Sakurai K., Yamasaki S., Hayashi K., Nagata C., Hoshino K., Onodera Y., Nishino K., Yamaguchi A. DIP original experiment: DIP-255182X Nature 2013 IMEx Structural basis for the inhibition of bacterial multidrug exporters. Phosphorylation-independent regulation of the diguanylate cyclase WspR. Phosphorylation-independent regulation of the diguanylate cyclase WspR. PLoS biology 2008 imex curation De N., Pirruccello M., Krasteva PV., Bae N., Raghavan RV., Sondermann H. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined De N., Pirruccello M., Krasteva PV., Bae N., Raghavan RV., Sondermann H. DIP original experiment: DIP-68378X PLoS biology 2008 IMEx Phosphorylation-independent regulation of the diguanylate cyclase WspR. Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Leiman PG., Basler M., Ramagopal UA., Bonanno JB., Sauder JM., Pukatzki S., Burley SK., Almo SC., Mekalanos JJ. Only protein-protein interactions ecolx Escherichia coli 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Leiman PG., Basler M., Ramagopal UA., Bonanno JB., Sauder JM., Pukatzki S., Burley SK., Almo SC., Mekalanos JJ. DIP original experiment: DIP-133828X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. Nature 2011 imex curation Huang CS., Ge P., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Huang CS., Ge P., Zhou ZH., Tong L. DIP original experiment: DIP-249466X Nature 2011 IMEx An unanticipated architecture of the 750-kDa α6β6 holoenzyme of 3-methylcrotonyl-CoA carboxylase. MgATP regulates allostery and fiber formation in IMPDHs. MgATP regulates allostery and fiber formation in IMPDHs. Structure (London, England : 1993) 2013 imex curation Labesse G., Alexandre T., Vaupré L., Salard-Arnaud I., Him JL., Raynal B., Bron P., Munier-Lehmann H. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Labesse G., Alexandre T., Vaupré L., Salard-Arnaud I., Him JL., Raynal B., Bron P., Munier-Lehmann H. DIP original experiment: DIP-252313X Structure (London, England : 1993) 2013 IMEx MgATP regulates allostery and fiber formation in IMPDHs. Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties. Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties. Structure (London, England : 1993) 2006 imex curation Hong BS., Yun MK., Zhang YM., Chohnan S., Rock CO., White SW., Jackowski S., Park HW., Leonardi R. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Hong BS., Yun MK., Zhang YM., Chohnan S., Rock CO., White SW., Jackowski S., Park HW., Leonardi R. DIP original experiment: DIP-66369X Structure (London, England : 1993) 2006 IMEx Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties. tsi2_pseae Immune protein Tsi2 tsi2 Anti-toxin protein Tsi2 PA2703 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MNLKPQTLMVAIQCVAARTRELDAQLQNDDPQNAAELEQLLVGYDLAADDLKNAYEQALGQYSGLPPYDRLIEEPAS DIP protein Q9I0D9 original sequence version: 66 q8gq91_pseai armR basR_3 DY940_15825 NCTC12924_04578 protein protein pseai Pseudomonas aeruginosa MRILLVEDDKLIGRGIVAGLHKHGIAVHHVGTAEEAEATHAEDTFHALVLDLGLPDRDGMELLASMRAVEPQLPVLILTARDAIEHRLKGLHEGADDYMIKPFDLRELAARLHALVRRTQGRAAQVISAGPLRLEPESGLAWFQGEPVSLSRREVDLLAHLANADGRWVPPDMLNERLYGLGEEIGSNALNVHIHNIRRKLGAEAIETVRGLGYRLGWRLAS DIP protein Q8GQ91 original sequence version: 33 psce_pseae Type III export protein PscE Pseudomonas secretion protein E PA1718 pscE protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MMTALETRLSVADGTHAAALRQRLQAALAECRRELARGACPEHFQFLQQQARALEGGLGILSQLTED DIP protein Q9I317 original sequence version: 66 62339AFECA931617 q9i1b2_pseae PA2367 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MDAIILDFGSDIKGDSLLVGYENKIEIMSYSHNVAMQVTNDVSNSERTSGKPHVGEFTLTKFIDTSTPTLNEYCCAGKPIAEATITIGRNAAEGNGQIMPFIVYTLNNVVLSNVSVSGGAGGKPVETLSLNFTKIKWELTAQKDDGTKEGTAASTWDLAANQLVK A4F50F0C183620E4 q9i6v6_pseae aer2 PA0176 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MGLFNAHAVAQQRADRIATLLQSFADGQLDTAVGEAPAPGYERLYDSLRALQRQLREQRAELQQVESLEAGLAEMSRQHEAGWIDQTIPAERLEGRAARIAKGVNELVAAHIAVKMKVVSVVTAYGQGNFEPLMDRLPGKKAQITEAIDGVRERLRGAAEATSAQLATAAYNARIKSALDNVSANVMIADNDLNIIYMNRTVSEMLGRAEADIRKQLPNFDAGRLMGANIDVFHKNPAHQRHLLANLTGVHKAELNLGGRRFSLDVVPVFNDANERLGSAVQWTDRTEEHRAEQEVSQLVQAAAAGDFSKRVEEAGKEGFFLRLAKDLNSLVDTADRGLRDVSRMLGALAQGDLTQRIEADYQGTFGQLKDFSNDTAQSLSRMLGQIREAADTINTAASEIASGNAELSARTEQQASSLEETASSMEELTSTVKLNAENARQANSLAANASEVATQGGTVVQKVVSTMSSINESARKIADIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLAQRSAAAAKEIKTLISDSVDKVENGNTLVAQAGQTMSDIVVAIRRVTDIMSEIAAASAEQSTGIEEVNSAVSQMDDMTQQNAALVEEAAAAAEAMQEQAGLLNQSVAVFRLDTPPSVVQLASARPSAPRPSAPAPLARSGMARASKARKEDGWEEF 246EF0D775120272 q9hxh5_pseae PA3827 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MVKLDRYIGVTVFVAILAVLGVILGLALLFAFIDELNDISASYGIGDALRFIFLTAPRRAYDMLPMAALIGCLVGLGTLASNSELTIMRAAGVSLSRIVWAVMKPMLVLMLAGILVGEYVAPWTENIAQSGRALAQGGGDSQSSKRGLWHRQGREYIHINAVQPNGVLYGVTRYRFDEQRGLESASFAKRARFETDHWQLEEVTTTLLHPREKRSEVVKLPTERWDAQLSPQLLNTVVMEPEALSISGLWQYIHYLADQGLNNNRYWLAFWTKVLQPLVTAALVLMAISFIFGPLRSVTLGQRIFTGVLVGFVFRIAQDLLGPSSLVFDFPPLLAVVIPASICALAGVWLLRRAG 506E7090975080B5 porp_pseae Porin P PA3279 oprP Outer membrane protein D1 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MIRRHSCKGVGSSVAWSLLGLAISAQSLAGTVTTDGADIVIKTKGGLEVATTDKEFSFKLGGRLQADYGRFDGYYTNNGNTADAAYFRRAYLEFGGTAYRDWKYQINYDLSRNVGNDSAGYFDEASVTYTGFNPVNLKFGRFYTDFGLEKATSSKWVTALERNLTYDIADWVNDNVGTGIQASSVVGGMAFLSGSVFSENNNDTDGDSVKRYNLRGVFAPLHEPGNVVHLGLQYAYRDLEDSAVDTRIRPRMGMRGVSTNGGNDAGSNGNRGLFGGSSAVEGLWKDDSVWGLEGAWALGAFSAQAEYLRRTVKAERDREDLKASGYYAQLAYTLTGEPRLYKLDGAKFDTIKPENKEIGAWELFYRYDSIKVEDDNIVVDSATREVGDAKGKTHTLGVNWYANEAVKVSANYVKAKTDKISNANGDDSGDGLVMRLQYVF 840243D11CDC7C26 mexr_pseae Multidrug resistance operon repressor mexR PA0424 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MNYPVNPDLMPALMAVFQHVRTRIQSELDCQRLDLTPPDVHVLKLIDEQRGLNLQDLGRQMCRDKALITRKIRELEGRNLVRRERNPSDQRSFQLFLTDEGLAIHQHAEAIMSRVHDELFAPLTPVEQATLVHLLDQCLAAQPLEDI 59F5146394BE89DD 59F5146394BE89DD ivy_pseae Inhibitor of vertebrate lysozyme ivy PA3902 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MNGVSRLLSLALLGAALHWAPAQAEEQPRLFELLGQPGYKATWHAMFKGESDVPKWVSDASGPSSPSTSLSLEGQPYVLANSCKPHDCGNNRLLVAFRGDKSAAYGLQVSLPDEPAEVMQTPSKYATYRWYGEPSRQVRELLMKQLESDPNWK DIP protein Q9HXB1 original sequence version: 74 rnt_pseae Ribonuclease T rnt Exoribonuclease T PA3528 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSEDNFDDEFDGSLPSGPRHPMARRFRGYLPVVVDVETGGFNSATDALLEIAATTVGMDEKGFLFPEHTYFFRIEPFEGANIEPAALEFTGIKLDHPLRMAVQEEAALTEIFRGIRKALKANGCKRAILVGHNSSFDLGFLNAAVARTGIKRNPFHPFSSFDTATLAGLAYGQTVLAKACQAAGMEFDNREAHSARYDTEKTAELFCGIVNRWKEMGGWMDDDD CC1010D3AD60F442 q9hvv6_pseae Lipopolysaccharide export system ATP-binding protein LptB PA4461 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MATLKAQHLAKSYKGRQVVRDVSMSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGVVRIDEQNVTHLPMHGRARAGIGYLPQEASIFRKLSVSDNIMAILETRSDLDRNGRKEALEGLLQEFHIHHIRDNLGMSLSGGERRRVEIARALASAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGILITDHNVRETLDICETAYIVNDGQLIAEGDAESILANDLVKEVYLGHEFRL A77C43C69317927A ubix_pseae Flavin prenyltransferase UbiX ubiX PA4019 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSGPERITLAMTGASGAQYGLRLLDCLVQEEREVHFLISKAAQLVMATETDVALPAKPQAMQAFLTEYCGAAAGQIRVFGQNDWMAPPASGSSAPNAMVICPCSTGTLSAVATGACNNLIERAADVALKERRPLVLVPREAPFSSIHLENMLKLSNLGAVILPAAPGFYHQPQSVEDLVDFVVARILNTLGIPQDMLPRWGEQHLVSDE DIP protein Q9HX08 original sequence version: 70 mexb_pseae Multidrug resistance protein MexB Multidrug-efflux transporter MexB PA0426 mexB protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSKFFIDRPIFAWVIALVIMLAGGLSILSLPVNQYPAIAPPAIAVQVSYPGASAETVQDTVVQVIEQQMNGIDNLRYISSESNSDGSMTITVTFEQGTDPDIAQVQVQNKLQLATPLLPQEVQRQGIRVTKAVKNFLMVVGVVSTDGSMTKEDLSNYIVSNIQDPLSRTKGVGDFQVFGSQYSMRIWLDPAKLNSYQLTPGDVSSAIQAQNVQISSGQLGGLPAVKGQQLNATIIGKTRLQTAEQFENILLKVNPDGSQVRLKDVADVGLGGQDYSINAQFNGSPASGIAIKLATGANALDTAKAIRQTIANLEPFMPQGMKVVYPYDTTPVVSASIHEVVKTLGEAILLVFLVMYLFLQNFRATLIPTIAVPVVLLGTFGVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVMAEEGLSPREAARKSMGQIQGALVGIAMVLSAVFLPMAFFGGSTGVIYRQFSITIVSAMALSVIVALILTPALCATMLKPIEKGDHGEHKGGFFGWFNRMFLSTTHGYERGVASILKHRAPYLLIYVVIVAGMIWMFTRIPTAFLPDEDQGVLFAQVQTPPGSSAERTQVVVDSMREYLLEKESSSVSSVFTVTGFNFAGRGQSSGMAFIMLKPWEERPGGENSVFELAKRAQMHFFSFKDAMVFAFAPPSVLELGNATGFDLFLQDQAGVGHEVLLQARNKFLMLAAQNPALQRVRPNGMSDEPQYKLEIDDEKASALGVSLADINSTVSIAWGSSYVNDFIDRGRVKRVYLQGRPDARMNPDDLSKWYVRNDKGEMVPFNAFATGKWEYGSPKLERYNGVPAMEILGEPAPGLSSGDAMAAVEEIVKQLPKGVGYSWTGLSYEERLSGSQAPALYALSLLVVFLCLAALYESWSIPFSVMLVVPLGVIGALLATSMRGLSNDVFFQVGLLTTIGLSAKNAILIVEFAKELHEQGKGIVEAAIEACRMRLRPIVMTSLAFILGVVPLAISTGAGSGSQHAIGTGVIGGMVTATVLAIFWVPLFYVAVSTLFKDEASKQQASVEKGQ DIP protein P52002 original sequence version: 92 FF91855338868ED2 q9i299_pseae liuD PA2012 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MNPDYRSIQRLLVANRGEIACRVMRSARALGIGSVAVHSDIDRHARHVAEADIAVDLGGAKPADSYLRGDRIIAAALASGAQAIHPGYGFLSENADFARACEEAGLLFLGPPAAAIDAMGSKSAAKALMEEAGVPLVPGYHGEAQDLETFRREAGRIGYPVLLKAAAGGGGKGMKVVEREAELAEALSSAQREAKAAFGDARMLVEKYLLKPRHVEIQVFADRHGHCLYLNERDCSIQRRHQKVVEEAPAPGLGAELRRAMGEAAVRAAQAIGYVGAGTVEFLLDERGQFFFMEMNTRLQVEHPVTEAITGLDLVAWQIRVARGEALPLTQEQVPLNGHAIEVRLYAEDPEGDFLPASGRLMLYREAAAGPGRRVDSGVREGDEVSPFYDPMLAKLIAWGETREEARQRLLAMLAETSVGGLRTNLAFLRRILGHPAFAAAELDTGFIARHQDDLLPAPQALPEHFWQAAAEAWLQSEPGHRRDDDPHSPWSRNDGWRSALARESDLMLRCRDERRCVRLRHASPSQYRLDGDDLVSRVDGVTRRSAALRRGRQLFLEWEGELLAIEAVDPIAEAEAAHAHQGGLSAPMNGSIVRVLVEPGQTVEAGATLVVLEAMKMEHSIRAPHAGVVKALYCSEGELVEEGTPLVELDENQA DIP protein Q9I299 original sequence version: 66 rure_pseae Rubredoxin-NAD(+) reductase alkT PA5349 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSERAPLVIIGTGLAGYNLAREWRKLDGETPLLMITADDGRSYSKPMLSTGFSKNKDADGLAMAEPGAMAEQLNARILTHTRVTGIDPGHQRIWIGEEEVRYRDLVLAWGAEPIRVPVEGDAQDALYPINDLEDYARFRQAAAGKRRVLLLGAGLIGCEFANDLSSGGYQLDVVAPCEQVMPGLLHPAAAKAVQAGLEGLGVRFHLGPVLASLKKAGEGLEAHLSDGEVIPCDLVVSAVGLRPRTELAFAAGLAVNRGIVVDRSLRTSHANIYALGDCAEVDGLNLLYVMPLMACARALAQTLAGNPSQVAYGPMPVTVKTPACPLVVSPPPRGMDGQWLVEGSGTDLKVLCRDTAGRVIGYALTGAAVNEKLALNKELPGLMA C98EA1FC3E15FA8F coax_pseae Type III pantothenate kinase coaX PanK-III Pantothenic acid kinase coaA PA4279 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MILELDCGNSLIKWRVIEGAARSVAGGLAESDDALVEQLTSQQALPVRACRLVSVRSEQETSQLVARLEQLFPVSALVASSGKQLAGVRNGYLDYQRLGLDRWLALVAAHHLAKKACLVIDLGTAVTSDLVAADGVHLGGYICPGMTLMRSQLRTHTRRIRYDDAEARRALASLQPGQATAEAVERGCLLMLRGFVREQYAMACELLGPDCEIFLTGGDAELVRDELAGARIMPDLVFVGLALACPIE 609D37480899DA3B pscf_pseae Type III needle protein PscF pscF Pseudomonas secretion protein F PA1719 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MAQIFNPNPGNTLDTVANALKEQANAANKDVNDAIKALQGTDNADNPALLAELQHKINKWSVIYNINSTVTRALRDLMQGILQKI DIP protein P95434 original sequence version: 78 32177F58EB7E37C4 pvdq_pseae Acyl-homoserine lactone acylase PvdQ pvdQ qsc112 PA2385 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MGMRTVLTGLAGMLLGSMMPVQADMPRPTGLAADIRWTAYGVPHIRAKDERGLGYGIGYAYARDNACLLAEEIVTARGERARYFGSEGKSSAELDNLPSDIFYAWLNQPEALQAFWQAQTPAVRQLLEGYAAGFNRFLREADGKTTSCLGQPWLRAIATDDLLRLTRRLLVEGGVGQFADALVAAAPPGAEKVALSGEQAFQVAEQRRQRFRLERGSNAIAVGSERSADGKGMLLANPHFPWNGAMRFYQMHLTIPGRLDVMGASLPGLPVVNIGFSRHLAWTHTVDTSSHFTLYRLALDPKDPRRYLVDGRSLPLEEKSVAIEVRGADGKLSRVEHKVYQSIYGPLVVWPGKLDWNRSEAYALRDANLENTRVLQQWYSINQASDVADLRRRVEALQGIPWVNTLAADEQGNALYMNQSVVPYLKPELIPACAIPQLVAEGLPALQGQDSRCAWSRDPAAAQAGITPAAQLPVLLRRDFVQNSNDSAWLTNPASPLQGFSPLVSQEKPIGPRARYALSRLQGKQPLEAKTLEEMVTANHVFSADQVLPDLLRLCRDNQGEKSLARACAALAQWDRGANLDSGSGFVYFQRFMQRFAELDGAWKEPFDAQRPLDTPQGIALDRPQVATQVRQALADAAAEVEKSGIPDGARWGDLQVSTRGQERIAIPGGDGHFGVYNAIQSVRKGDHLEVVGGTSYIQLVTFPEEGPKARGLLAFSQSSDPRSPHYRDQTELFSRQQWQTLPFSDRQIDADPQLQRLSIRE 8CAD38D280EDD43B q9hvv8_pseae Lipopolysaccharide export system protein LptC lptC PA4459 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MPKTLRQKLLLALIALLLIVAGYYWNVGLELFNEQPTRPGQDNTIDYYAENAHSLQYQEDGSLDYEMTAVKLEHQKATDITFVTTPDLLLFRGNVQPWHIQSARAEVGPKGKEVELIDDVRVARTDAKGQPSILTTTRLTVFPDKNYAQTEQAVKIDAANGVTTAVGMKAYLKDSRMHLLSNVRGQHEVR 5CB84CE5F41A8AE3 maje_pseae Major exported protein hcpA hcpB hcpC Secreted protein hcp PA0263 PA1512 PA5267 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MATPAYMSITGTKQGLITAGAFTEDSVGNTYQEGHEDQVMVQGFNHEVIIPRDPQSGQPTGQRVHKPVVITKVFDKASPLLLAALTSGERLTKVEIQWYRTSAAGTQEHYYTTVLEDAIIVDIKDYMHNCQDPGNAHFTHLEDVHFTYRKITWTHEVSGTSGSDDWRSPVAG 8565ABE2F64B9577 q9hxt9_pseae wspR PA3702 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MHNPHESKTDLGAPLDGAVMVLLVDDQAMIGEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYIALQQRDEAYRALRESQQQLLETNLVLQRLMNSDGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREGCSRSSDLAARYGGEEFAMVLPGTSPGGARLLAEKVRRTVESLQISHDQPRPGSHLTVSIGVSTLVPGGGGQTFRVLIEMADQALYQAKNNGRNQVGLMEQPVPPAPAG AE706D630586649E azur_pseae Azurin azu PA4922 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MLRKLAAVSLLSLLSAPLLAAECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTFPGHSALMKGTLTLK 9C3881D7B6D64B67 mint 9C3881D7B6D64B67 flicb_pseae B-type flagellin fliC PA1092 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MALTVNTNIASLNTQRNLNASSNDLNTSLQRLTTGYRINSAKDDAAGLQISNRLSNQISGLNVATRNANDGISLAQTAEGALQQSTNILQRIRDLALQSANGSNSDADRAALQKEVAAQQAELTRISDTTTFGGRKLLDGSFGTTSFQVGSNAYETIDISLQNASASAIGSYQVGSNGAGTVASVAGTATASGIASGTVNLVGGGQVKNIAIAAGDSAKAIAEKMDGAIPNLSARARTVFTADVSGVTGGSLNFDVTVGSNTVSLAGVTSTQDLADQLNSNSSKLGITASINDKGVLTITSATGENVKFGAQTGTATAGQVAVKVQGSDGKFEAAAKNVVAAGTAATTTIVTGYVQLNSPTAYSVSGTGTQASQVFGNASAAQKSSVASVDISTADGAQNAIAVVDNALAAIDAQRADLGAVQNRFKNTIDNLTNISENATNARSRIKDTDFAAETAALSKNQVLQQAGTAILAQANQLPQAVLSLLR 7A2AEE09D3F58209 oprm_pseae Outer membrane protein OprM oprM oprK PA0427 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MKRSFLSLAVAAVVLSGCSLIPDYQRPEAPVAAAYPQGQAYGQNTGAAAVPAADIGWREFFRDPQLQQLIGVALENNRDLRVAALNVEAFRAQYRIQRADLFPRIGVDGSGTRQRLPGDLSTTGSPAISSQYGVTLGTTAWELDLFGRLRSLRDQALEQYLATEQAQRSAQTTLVASVATAYLTLKADQAQLQLTKDTLGTYQKSFDLTQRSYDVGVASALDLRQAQTAVEGARATLAQYTRLVAQDQNALVLLLGSGIPANLPQGLGLDQTLLTEVPAGLPSDLLQRRPDILEAEHQLMAANASIGAARAAFFPSISLTANAGTMSRQLSGLFDAGSGSWLFQPSINLPIFTAGSLRASLDYAKIQKDINVAQYEKAIQTAFQEVADGLAARGTFTEQLQAQRDLVKASDEYYQLADKRYRTGVDNYLTLLDAQRSLFTAQQQLITDRLNQLTSEVNLYKALGGGWNQQTVTQQQTAKKEDPQA 7B0918E4FE7843EF q9huk6_pseae fimX PA4959 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MAIEKKTIRLLILEDSQNEAERLVSLFRNAGHATRVHRLTSPEDLAETLQQSWDLLIAAPTSECLEPGEALATLRRQSRDIPFIQLVADNSSDAITDALMLGAQDALPQGEDERLVLVANRELAGLAERRARRAAELALREAEKRCQLLLDSSVDAITYVHDGMHIYANRSYMALFGYEDAEELEGLPVIDLIASCDQGAFKDFLKGYQNDQRQTELVCTGVKLDGQEFKARISLSAATYDGEPCIQVVIRGEVDNAELEEKLREVSSQDPVTGLYNRSHFLDLMDAAVQQAVTARKPSTLAYIHLNGYPSLQADHGLSGIDLLLGQLAGLMREQFGEEADLARFGDSIFAALFKGKTPEQAQAALQRLLKKVENHLFELNGRSAQATLSIGVAGLDEKTAKAQDVMNRAHRCADDAARKGGSQIKQYNPAEELAAAAQRGDVIAILQQALETNSFRLLFQPVISLRGDSHENYEVLLRLLNPQGQEVPPAEFLHAAKEAGLAEKIDRWVILNSIKLLAEHRAKGHQTKLFVHLSSASLQDPGLLPWLGVALKAARLPPESLVFQISEADATSYLKQAKQLTQGLATLHCQAAISQFGCSLNPFNALKHLTVQFIKIDGSFVQDLNQVENQEILKGLIAELHEQQKLSIVPFVESASVLATLWQAGATYIQGYYLQGPSQAMDYDFSSGDE 518BAFE4C8977B43 q9i5i9_pseae sdsA1 PA0740 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSRLLALLALAPLLAGAAETTAPKPPSAFTVEAQRRVEAELPFADRADFERADRGLIRRPERLLIRNPDGSVAWQLGGYDFLLDGKPRDSINPSLQRQALLNLKYGLFEVAEGIYQVRGFDLANITFIRGDSGWIVVDTLTTPATARAAYELVSRELGERPIRTVIYSHAHADHFGGVRGLVEPQQVASGAVQIIAPAGFMEAAIKENVLAGNAMMRRATYQYGTQLPKGPQGQVDMAIGKGLARGPLSLLAPTRLIEGEGEDLVLDGVPFTFQNTPGTESPAEMNIWLPRQKALLMAENVVGTLHNLYTLRGAEVRDALGWSKYINQALHRFGRQAEVMFAVHNWPRWGNAEIVEVLEKQRDLYGYLHDQTLHLANQGVTIGQVHNRLRLPPSLDQEWYDRGYHGSVSHNARAVLNRYLGYYDGNPATLDPLSPEDSAGRYVEYMGGAERLLEQARASYARGEYRWVVEVVNRLVFAEPDNRAARELQADALEQLGYQAENAGWRNSYLSAAYELRHGVPRDQPTMKAGSADALAAMDTGLLFDYLGVRLDAGAAEGKALSINLRLPDIGENYLLELKNSHLNNLRGVQSEDAGQTVSIDRADLNRLLLKEVSAVRLVFEGKLKSSGNPLLLGQLFGMLGDFDFWFDIVTPAAKSEG DIP protein Q9I5I9 original sequence version: 85 3D29B5D2B0A2A84F q9hxh4_pseae Lipopolysaccharide export system permease protein LptF PA3828 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MIVFRYLSREVLVTMSAVSAVLLVIIMSGRFIKYLAQAAQGLLDPGSLFLIMAFRIPGFLQLILPLGLFLGILLAYGRLYLESEMTVLSATGMSQKRLLGYTMAPALLVAILVAWLSLFLAPQGINQFALLLNKQDTLTEFDTLVPGRFQAMRDGTRVTYTEELSKDRGELAGIFISQKDLNSSNQERGISILVAEKGTQNIQADGSRYLILHNGYRYDGNPGQANYRAIQYDTYGVMLPKPEASSEVSERDAVPTADLFGSDNPRYQAELQWRLSTPLLVFVVTLLAVPLSRVNPRQGRFLKLLPAILLYMGYLALLIAVRGQLDKGKIPMAIGLWWVHGLFLAIGLLLFYWEPLRLKLASSRAGREVAHG 38708A52C695846C pord_pseae Porin D oprD Imipenem/basic amino acid-specific outer membrane pore Outer membrane protein D2 PA0958 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MKVMKWSAIALAVSAGSTQFAVADAFVSDQAEAKGFIEDSSLDLLLRNYYFNRDGKSGSGDRVDWTQGFLTTYESGFTQGTVGFGVDAFGYLGLKLDGTSDKTGTGNLPVMNDGKPRDDYSRAGGAVKVRISKTMLKWGEMQPTAPVFAAGGSRLFPQTATGFQLQSSEFEGLDLEAGHFTEGKEPTTVKSRGELYATYAGETAKSADFIGGRYAITDNLSASLYGAELEDIYRQYYLNSNYTIPLASDQSLGFDFNIYRTNDEGKAKAGDISNTTWSLAAAYTLDAHTFTLAYQKVHGDQPFDYIGFGRNGSGAGGDSIFLANSVQYSDFNGPGEKSWQARYDLNLASYGVPGLTFMVRYINGKDIDGTKMSDNNVGYKNYGYGEDGKHHETNLEAKYVVQSGPAKDLSFRIRQAWHRANADQGEGDQNEFRLIVDYPLSIL E083FFE074DCFB64 hcp1_pseae Protein hcp1 hcp1 PA0085 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MAVDMFIKIGDVKGESKDKTHAEEIDVLAWSWGMSQSGSMHMGGGGGAGKVNVQDLSFTKYIDKSTPNLMMACSSGKHYPQAKLTIRKAGGENQVEYLIITLKEVLVSSVSTGGSGGEDRLTENVTLNFAQVQVDYQPQKADGAKDGGPVKYGWNIRQNVQA BFC45EC5C8107BF5 tse2_pseae Toxin Tse2 tse2 PA2702 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSYDYEKTSLTLYRAVFKANYDGDVGRYLHPDKELAEAAEVAPLLHPTFDSPNTPGVPARAPDIVAGRDGLYAPDTGGTSVFDRAGVLRRADGDFVIPDGTDIPPDLKVKQDSYNKRLQATHYTIMPAKPMYREVLMGQLDNFVRNAIRRQWEKARGL DIP protein Q9I0E0 original sequence version: 56 gspd_pseae Secretin XcpQ xcpQ General secretion pathway protein D Type II secretion system protein D PA3105 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSQPLLRALFAPSSRSYVPAVLLSLALGIQAAHAENSGGNAFVPAGNQQEAHWTINLKDADIREFIDQISEITGETFVVDPRVKGQVSVVSKAQLSLSEVYQLFLSVMSTHGFTVVAQGDQARIVPNAEAKTEAGGGQSAPDRLETRVIQVQQSPVSELIPLIRPLVPQYGHLAAVPSANALIISDRSANIARIEDVIRQLDQKGSHDYSVINLRYGWVMDAAEVLNNAMSRGQAKGAAGAQVIADARTNRLIILGPPQARAKLVQLAQSLDTPTARSANTRVIRLRHNDAKTLAETLGQISEGMKNNGGQGGEQTGGGRPSNILIRADESTNALVLLADPDTVNALEDIVRQLDVPRAQVLVEAAIVEISGDIQDAVGVQWAINKGGMGGTKTNFANTGLSIGTLLQSLESNKAPESIPDGAIVGIGSSSFGALVTALSANTKSNLLSTPSLLTLDNQKAEILVGQNVPFQTGSYTTNSEGSSNPFTTVERKDIGVSLKVTPHINDGAALRLEIEQEISALLPNAQQRNNTDLITSKRSIKSTILAENGQVIVIGGLIQDDVSQAESKVPLLGDIPLLGRLFRSTKDTHTKRNLMVFLRPTVVRDSAGLAALSGKKYSDIRVIDGTRGPEGRPSILPTNANQLFDGQAVDLRELMTE DIP protein P35818 original sequence version: 98 q9hxm5_pseae Inosine-5'-monophosphate dehydrogenase guaB PA3770 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MLRISQEALTFDDVLLIPGYSEVLPKDVSLKTRLTRGIELNIPLVSAAMDTVTEARLAIAMAQEGGIGIIHKNMGIEQQAAEVRKVKKHETAIVRDPVTVTPSTKIIELLQMAREYGFSGFPVVEQGELVGIVTGRDLRVKPNAGDTVAAIMTPKDKLVTAREGTPLEEMKAKLYENRIEKMLVVDENFYLRGLVTFRDIEKAKTYPLASKDEQGRLRVGAAVGTGADTGERVAALVAAGVDVVVVDTAHGHSKGVIERVRWVKQTFPDVQVIGGNIATAEAAKALAEAGADAVKVGIGPGSICTTRIVAGVGVPQISAIANVAAALEGTGVPLIADGGIRFSGDLAKAMVAGAYCVMMGSMFAGTEEAPGEIELFQGRSYKSYRGMGSLGAMSGSQGSSDRYFQDASAGAEKLVPEGIEGRVPYKGALSAIVHQLMGGLRAAMGYTGSADIQQMRTQPQFVRITGAGMAESHVHDVQITKEAPNYRVG DIP protein Q9HXM5 original sequence version: 86 pscg_pseae Type III export protein PscG Pseudomonas secretion protein G PA1720 pscG protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MDTSLIRELAELALAGSGQHCHEEALCIAEWLERLGQDEAARLIRISSLANQGRYQEALAFAHGNPWPALEPWFALCEWHLGLGAALDRRLAGLGGSSDPALADFAAGMRAQVRT DIP protein P95435 original sequence version: 75 3F546AA0645050B7 lysc_chick Lysozyme C LYZ 1,4-beta-N-acetylmuramidase C Allergen Gal d IV protein protein chick Gallus gallus (Chicken) Chicken MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL DIP protein P00698 original sequence version: 158 81E85743FF579468 rubr2_pseae Rubredoxin-2 rubA2 alkG2 PA5350 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MRKWQCVVCGFIYDEALGLPEEGIPAGTRWEDIPADWVCPDCGVGKIDFEMIEIA 9C27F01DAB7E49C6 faby_pseae Beta-ketoacyl-[acyl-carrier-protein] synthase FabY fabY Beta-ketoacyl synthase KAS I/II domain-containing enzyme PA5174 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSRLPVIVGFGGYNAAGRSSFHHGFRRMVIESMDPQARQETLAGLAVMMKLVKAEGGRYLAEDGTPLSPEDIERRYAERIFASTLVRRIEPQYLDPDAVHWHKVLELSPAEGQALTFKASPKQLPEPLPANWSIAPAEDGEVLVSIHERCEFKVDSYRALTVKSAGQLPTGFEPGELYNSRFHPRGLQMSVVAATDAIRSTGIDWKTIVDNVQPDEIAVFSGSIMSQLDDNGFGGLMQSRLKGHRVSAKQLPLGFNSMPTDFINAYVLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATEEGLRLIEGRDDVDFRRASRPFGENCGFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGFKKSISAPGPGNYLTVAKAVASAVQIVGLDTVRHASFVHAHGSSTPANRVTESEILDRVASAFGIDGWPVTAVKAYVGHSLATASADQLISALGTFKYGILPGIKTIDKVADDVHQQRLSISNRDMRQDKPLEVCFINSKGFGGNNASGVVLSPRIAEKMLRKRHGQAAFAAYVEKREQTRAAARAYDQRALQGDLEIIYNFGQDLIDEHAIEVSAEQVTVPGFSQPLVYKKDARFSDMLD DIP protein Q9HU15 original sequence version: 76 bphy_pseae Bacteriophytochrome bphP Phytochrome-like protein PA4117 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MTSITPVTLANCEDEPIHVPGAIQPHGALVTLRADGMVLAASENIQALLGFVASPGSYLTQEQVGPEVLRMLEEGLTGNGPWSNSVETRIGEHLFDVIGHSYKEVFYLEFEIRTADTLSITSFTLNAQRIIAQVQLHNDTASLLSNVTDELRRMTGYDRVMAYRFRHDDSGEVVAESRREDLESYLGQRYPASDIPAQARRLYIQNPIRLIADVAYTPMRVFPALNPETNESFDLSYSVLRSVSPIHCEYLTNMGVRASMSISIVVGGKLWGLFSCHHMSPKLIPYPVRMSFQIFSQVCSAIVERLEQGRIAELLRVSTERRLALARRARDADDLFGALAHPDDGIAALIPCDGALVMLGGRTLSIRGDFERQAGNVLQRLQRDPERDIYHTDNWPQPSEDSPDGGDCCGVLAIRFHRQESGWIFWFRHEEVHRIRWGGKPEKLLTIGPSGPRLTPRGSFEAWEEVVRGHSTPWSETDLAIAEKLRLDLMELCLNHAAEVDRMRQRLIAVLGHDLRNPLQSISMAAALLSSSDTRTTELRQHISASSSRMERLVSQILDMSRLQSGIGLTVNPVDTDVSQLVRQIVCETDVAYPGLVIEIAIDPQVRAVVDPDRYAQVAANLLSNARHHGLPGRPVLVTLTRQGDEVCLSVLNETSGLSEAQLANLFEPFKRESADNQRNRNGLGIGLYISQAIAQAHQGRIDVDCRDDVITFCLRLPVRQAETGSSS EEE9259392E5C4B0 pk22_pseae Polyphosphate:AMP phosphotransferase Polyphosphate kinase PPK2 3 PA3455 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MFESAEVGHSIDKDTYEKAVIELREALLEAQFELKQQARFPVIILINGIEGAGKGETVKLLNEWMDPRLIEVQSFLRPSDEELERPPQWRFWRRLPPKGRTGIFFGNWYSQMLYARVEGHIKEAKLDQAIDAAERFERMLCDEGALLFKFWFHLSKKQLKERLKALEKDPQHSWKLSPLDWKQSEVYDRFVHYGERVLRRTSRDYAPWYVVEGADERYRALTVGRILLEGLQAALATKERAKRQPHAAPLVSSLDNRGLLDSLDLGQYLDKDAYKEQLAAEQARLAGLIRDKRFRQHSLVAVFEGNDAAGKGGAIRRVTDALDPRQYHIVPIAAPTEEERAQPYLWRFWRHIPARRQFTIFDRSWYGRVLVERIEGFCAPADWLRAYGEINDFEEQLSEYGIIVVKFWLAIDKQTQMERFKEREKTPYKRYKITEEDWRNRDKWDQYVDAVGDMVDRTSTEIAPWTLVEANDKRFARVKVLRTINDAIEAAYKKDK 6BA1C283EA5C53E5 bir1e_mouse Baculoviral IAP repeat-containing protein 1e Naip5 Birc1e Naip-rs3 Neuronal apoptosis inhibitory protein 5 protein protein mouse Mus musculus Mouse MAEHGESSEDRISEIDYEFLPELSALLGVDAFQVAKSQEEEEHKERMKMKKGFNSQMRSEAKRLKTFETYDTFRSWTPQEMAAAGFYHTGVRLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQGKDVGNIGKYDIRVKRPEKMLRGGKARYHEEEARLESFEDWPFYAHGTSPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQSKKSSEEIAQYIQSYEGFVHVTGEHFVKSWVRRELPMVSAYCNDSVFANEELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQTLKSSAEVIPTLQSQYALPEATETTRESNHGDAAAVHSTVVDLGRSEAQWFQEARSLSEQLRDNYTKATFRHMNLPEVCSSLGTDHLLSCDVSIISKHISQPVQEALTIPEVFSNLNSVMCVEGETGSGKTTFLKRIAFLWASGCCPLLYRFQLVFYLSLSSITPDQGLANIICAQLLGAGGCISEVCLSSSIQQLQHQVLFLLDDYSGLASLPQALHTLITKNYLSRTCLLIAVHTNRVRDIRLYLGTSLEIQEFPFYNTVSVLRKFFSHDIICVEKLIIYFIDNKDLQGVYKTPLFVAAVCTDWIQNASAQDKFQDVTLFQSYMQYLSLKYKATAEPLQATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDEKLTTLLMSKFTAQRLRPVYRFLGPLFQEFLAAVRLTELLSSDRQEDQDLGLYYLRQIDSPLKAINSFNIFLYYVSSHSSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPQTFLWFQFVRGLWLVSPESSSSFVSEHLLRLALIFAYESNTVAECSPFILQFLRGKTLALRVLNLQYFRDHPESLLLLRSLKVSINGNKMSSYVDYSFKTYFENLQPPAIDEEYTSAFEHISEWRRNFAQDEEIIKNYENIRPRALPDISEGYWKLSPKPCKIPKLEVQVNNTDAADQALLQVLMEVFSASQSIEFRLFNSSGFLESICPALELSKASVTKCSMSRLELSRAEQELLLTLPALQSLEVSETNQLPEQLFHNLHKFLGLKELCVRLDGKPNVLSVLPREFPNLLHMEKLSIQTSTESDLSKLVKFIQNFPNLHVFHLKCDFLSNCESLMAVLASCKKLREIEFSGRCFEAMTFVNILPNFVSLKILNLKDQQFPDKETSEKFAQALGSLRNLEELLVPTGDGIHQVAKLIVRQCLQLPCLRVLTFHDILDDDSVIEIARAATSGGFQKLENLDISMNHKITEEGYRNFFQALDNLPNLQELNICRNIPGRIQVQATTVKALGQCVSRLPSLIRLHMLSWLLDEEDMKVINDVKERHPQSKRLIIFWKLIVPFSPVILE DIP protein Q9R016 original sequence version: 82 DIP protein Q9R016 original sequence version: 113 DIP protein Q9R016 original sequence version: 118 DIP protein Q9R016 original sequence version: 115 04C04877908103EE q9i297_pseae liuB PA2014 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MAILHTQINPRSAEFAANAATMLEQVNALRTLLGRIHEGGGSAAQARHSARGKLLVRERINRLLDPGSPFLELSALAAHEVYGEEVAAAGIVAGIGRVEGVECMIVGNDATVKGGTYYPLTVKKHLRAQAIALENRLPCIYLVDSGGANLPRQDEVFPDREHFGRIFFNQANMSARGIPQIAVVMGSCTAGGAYVPAMSDETVMVREQATIFLAGPPLVKAATGEVVSAEELGGADVHCKVSGVADHYAEDDDHALAIARRCVANLNWRKQGQLQCRAPRAPLYPAEELYGVIPADSKQPYDVREVIARLVDGSEFDEFKALFGTTLVCGFAHLHGYPIAILANNGILFAEAAQKGAHFIELACQRGIPLLFLQNITGFMVGQKYEAGGIAKHGAKLVTAVACARVPKFTVLIGGSFGAGNYGMCGRAYDPRFLWMWPNARIGVMGGEQAAGVLAQVKREQAERAGQQLGVEEEAKIKAPILEQYEHQGHPYYSSARLWDDGVIDPAQTREVLALALSAALNAPIEPTAFGVFRM DIP protein Q9I297 original sequence version: 42 q9hus3_pseae desT PA4890 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSSPRAEQKQQTRHALMSAARHLMESGRGFGSLSLREVTRAAGIVPAGFYRHFSDMDQLGLALVAEVDETFRATLRAVRRNEFELGGLIDASVRIFLDAVGANRSQFLFLAREQYGGSLPIRQAIASLRQRITDDLAADLALLNKMPHLDGAALDVFADLVVKTVFATLPELIDPPAADLPPHLMPAAKITHQLRFIMIGGKHWHGLPG CE3EE8F29C0D0C1A sdsa1-6 16 90 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction sdsa1-7 39 90 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pacoaa-1 64 80 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction oprp-1 32 71 unspecified role unspecified role neutral component neutral component 3-410 binding region 3-410 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain pseai Pseudomonas aeruginosa physical association physical association ivy-lyz-2 36 73 unspecified role unspecified role unspecified role unspecified role Region 25-153 Region 25-153 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 98 unspecified role unspecified role unspecified role unspecified role Region 19-147 Region 19-147 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chick Gallus gallus (Chicken) Chicken direct interaction direct interaction prnase t-prnase t-1 19 74 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 74 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction psce-pscf-1 52 81 unspecified role unspecified role unspecified role unspecified role Region 55-85 Region 55-85 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 97 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 67 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction psce-pscf-2 50 81 unspecified role unspecified role unspecified role unspecified role Region 55-85 Region 55-85 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 97 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 67 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association rdxr-1 33 79 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction rdx-rdxr-1 43 99 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 79 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction rdx-rdxr-2 24 99 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 79 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction oprd-1 40 92 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli direct interaction direct interaction hcp1-1 46 93 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction hcp1-2 34 93 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction hcp1-3 25 93 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction wspr-1 41 85 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction wspr-2 60 85 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction wspr-3 37 85 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pabphp-1 53 101 unspecified role unspecified role unspecified role unspecified role Region 1-497 Region 1-497 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction armr-mexr-2 12 66 unspecified role unspecified role unspecified role unspecified role Region 29-53 Region 29-53 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 72 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction armr-mexr-3 35 66 unspecified role unspecified role unspecified role unspecified role Region 29-53 Region 29-53 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 72 unspecified role unspecified role unspecified role unspecified role Region 1-142 Region 1-142 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction armr-mexr-4 1 66 unspecified role unspecified role unspecified role unspecified role Region 29-53 Region 29-53 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 72 unspecified role unspecified role unspecified role unspecified role Region 1-142 Region 1-142 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction armr-mexr-5 2 66 unspecified role unspecified role unspecified role unspecified role Region 41-53 Region 41-53 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 72 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction armr-mexr-6 3 66 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 72 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pa3455-1 13 102 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pa3455-2 28 102 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction hcp3-1 61 68 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction hcp2-1 30 84 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction az-1 49 86 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction fimx-1 29 89 unspecified role unspecified role unspecified role unspecified role Region 1-431 Region 1-431 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fimx-2 5 89 unspecified role unspecified role unspecified role unspecified role Region 1-431 Region 1-431 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fimx-3 57 89 unspecified role unspecified role unspecified role unspecified role Region 1-431 Region 1-431 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pabphp-2 11 101 unspecified role unspecified role unspecified role unspecified role Region 1-497 Region 1-497 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pvdq-pvdq-1 31 82 unspecified role unspecified role unspecified role unspecified role PvdQ beta subunit Region 217-762 polyprotein frag polyprotein fragment polyprotein frag certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 82 unspecified role unspecified role unspecified role unspecified role PvdQ alpha subunit Region 24-193 polyprotein frag polyprotein fragment polyprotein frag certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pvdq-pvdq-2 14 82 unspecified role unspecified role unspecified role unspecified role PvdQ beta subunit Region 217-762 polyprotein frag polyprotein fragment polyprotein frag certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 82 unspecified role unspecified role unspecified role unspecified role PvdQ alpha subunit Region 24-193 polyprotein frag polyprotein fragment polyprotein frag certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pvdq-pvdq-3 27 82 unspecified role unspecified role unspecified role unspecified role PvdQ beta subunit Region 217-762 polyprotein frag polyprotein fragment polyprotein frag certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 82 unspecified role unspecified role unspecified role unspecified role PvdQ alpha subunit Region 24-193 polyprotein frag polyprotein fragment polyprotein frag certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction hamp-1 42 69 unspecified role unspecified role unspecified role unspecified role HAMP1-3 domain Region 1-172 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction hamp-2 23 69 unspecified role unspecified role unspecified role unspecified role HAMP1-3 domain Region 1-172 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction oprm-1 51 88 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction dest-1 15 105 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction paflic-naip5-1 10 87 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 103 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast direct interaction direct interaction bphp-4 58 101 unspecified role unspecified role unspecified role unspecified role Region 1-497 Region 1-497 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction bphp-5 21 101 putative self putative self unspecified role unspecified role Q9HWR3:p.Ser261Ala S261A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S A This feature has been corrected as a result of our quality control procedures. The original label was 'S261A'. Wed May 02 17:32:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser261ala' Tue Jun 30 19:43:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser261Ala' ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation true liub-liud-1 54 104 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 78 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction liub-liud-2 62 104 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 78 unspecified role unspecified role prey prey ecolx Escherichia coli physical association physical association liub-liud-3 4 104 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 78 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction liub-1 17 104 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction liub-liud-4 45 104 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 78 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction aer2-1 9 69 unspecified role unspecified role unspecified role unspecified role Region 1-172 Region 1-172 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction aer2-2 26 69 unspecified role unspecified role unspecified role unspecified role Region 1-172 Region 1-172 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain MTSSL-label MTSSL-label r1 spin label r1 spin label certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction aer2-3 8 69 unspecified role unspecified role unspecified role unspecified role Region 1-172 Region 1-172 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain MTSSL-label MTSSL-label r1 spin label r1 spin label certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction guab-1 22 96 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction guab-2 6 96 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction guab-3 18 96 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction guab-4 55 96 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction guab-5 63 96 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mexb-1 59 77 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction faby-1 44 100 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ubix-1 38 76 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction q9i0d9_pseae-q9i0e0_pseae-1 7 94 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 65 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction xcpq-1 56 95 unspecified role unspecified role unspecified role unspecified role in vitro In vitro direct interaction direct interaction xcpq-2 47 95 unspecified role unspecified role unspecified role unspecified role in vitro In vitro direct interaction direct interaction q9hvv6_pseae-q9hxh4_pseae-1 20 70 structure determination identification by structure determination identification by structure determination structure determination predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) 91 structure determination identification by structure determination identification by structure determination structure determination predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 75 structure determination identification by structure determination identification by structure determination structure determination predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) physical association physical association FIgure 1, Table 1 q9hvv6_pseae-q9hxh4_pseae-2 48 83 predetermined predetermined participant predetermined western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified ecoli Escherichia coli (strain K12) 70 predetermined predetermined participant predetermined western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified ecoli Escherichia coli (strain K12) 91 predetermined predetermined participant predetermined western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified ecoli Escherichia coli (strain K12) 75 predetermined predetermined participant predetermined western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait purified purified his tag his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) association association Figure 2 q9hvv6_pseae-lptc-1 48 70 predetermined predetermined participant predetermined western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified ecoli Escherichia coli (strain K12) 91 predetermined predetermined participant predetermined western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified ecoli Escherichia coli (strain K12) 75 predetermined predetermined participant predetermined western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait purified purified his tag his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) association association Figure 2 q9hvv6_pseae-q9hxh4_pseae-3 48 70 predetermined predetermined participant predetermined western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified ecoli Escherichia coli (strain K12) 91 predetermined predetermined participant predetermined western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified ecoli Escherichia coli (strain K12) 75 predetermined predetermined participant predetermined western blot western blot Immuno blot Immuno blot experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait purified purified his tag his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range Q9HVV6:p.Glu163Gln E163Q mutation mutation certain certain sequence position certain certain certain sequence position certain E Q Tue Jun 30 16:25:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu163Gln' ecoli Escherichia coli (strain K12) association association Figure 2 MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it A Pseudomonas aeruginosa type VI secretion system regulated by CueR facilitates copper acquisition. A Pseudomonas aeruginosa type VI secretion system regulated by CueR facilitates copper acquisition. PLoS pathogens 2019 imex curation Han Y., Wang T., Chen G., Pu Q., Liu Q., Zhang Y., Xu L., Wu M., Liang H. lianghh@nwu.edu.cn 13-Nov-2020: Contacted by IntAct-Help. Only protein-protein interactions imex curation pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Han Y., Wang T., Chen G., Pu Q., Liu Q., Zhang Y., Xu L., Wu M., Liang H. lianghh@nwu.edu.cn Accepted 2020-OCT-05 AT 16:19 BST AT 16:19 BST by KALPANAP PLoS pathogens 2019 Only protein-protein interactions imex curation imex curation A Pseudomonas aeruginosa type VI secretion system regulated by CueR facilitates copper acquisition. A Pseudomonas aeruginosa type VI secretion system regulated by CueR facilitates copper acquisition. PLoS pathogens 2019 imex curation Han Y., Wang T., Chen G., Pu Q., Liu Q., Zhang Y., Xu L., Wu M., Liang H. lianghh@nwu.edu.cn 13-Nov-2020: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro pull down pull down ms participant Identification by mass spectrometry ms participant Han Y., Wang T., Chen G., Pu Q., Liu Q., Zhang Y., Xu L., Wu M., Liang H. lianghh@nwu.edu.cn Accepted 2020-OCT-05 AT 16:19 BST AT 16:19 BST by KALPANAP PLoS pathogens 2019 Only protein-protein interactions imex curation imex curation A Pseudomonas aeruginosa type VI secretion system regulated by CueR facilitates copper acquisition. A Pseudomonas aeruginosa type VI secretion system regulated by CueR facilitates copper acquisition. PLoS pathogens 2019 imex curation Han Y., Wang T., Chen G., Pu Q., Liu Q., Zhang Y., Xu L., Wu M., Liang H. lianghh@nwu.edu.cn 13-Nov-2020: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro pull down pull down anti tag western anti tag western blot anti tag western Han Y., Wang T., Chen G., Pu Q., Liu Q., Zhang Y., Xu L., Wu M., Liang H. lianghh@nwu.edu.cn Accepted 2020-OCT-05 AT 16:19 BST AT 16:19 BST by KALPANAP PLoS pathogens 2019 Only protein-protein interactions imex curation imex curation g3xd89_pseae oprC PA3790 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MEKRMSTQQRAAGNACPTAAFSFDPARLAQRRRWAGAFAALCGLALSPSALLAEEHSQHQDHAVELAPSVVTGVAQSSPLTIVTNPKEPRQPVPASDGADYLKTIPGFAVIRNGGSNGDPVLRGMFGSRLNILTNGGMMLGACPNRMDAPTSYISPETYDKLTVIKGPQTVLWGPGASAGTILFEREPERFGELGSRVNASLLAGSNGRFDKVLDAAAGNRLGYLRFTGNHAQSDDYEDGAGNTVPSRWKKWNGDVAVGWTPDEDTLIELTAGKGDGEARYAGRGMDGSQFKRESLGLRFVKSNVSDVLEKVEAQVYYNYADHIMDNFRLRTPDPSSMMPMPMASQVDRRTLGGRLAATWRWDDFKLVTGVDAMRNEHRARGSKYDMMTDYYTDADQFPWSKDAVFHNYGAFGELTWFAAERDRLIGGLRLDRASVKDYRQTLKSGHMGHAMANPTANDTRADTLPSGFVRYEHDLADSPTTLYAGLGHAERFPDYWELFSPKRGPNGSVNAFDKIKPEKTTQLDFGLQYNGDKLQAWASGYVGVVQDFILFSYREGMMGSSTQATNVDARIMGGELGASYQLTGNWKTDASLAYAWGKNSSDDRALPQIPPLEARFGLTYEEGDWSAGSLWRVVAPQNRIARDQGNVVGKDFDKSAGFGVFSLNGAYRVTRNVKLSAGVDNLFDKDYTEHLNKAGDAGFGFSANETVPEPGRTFWTKVDFSF E9FC33618E830A3E eftu_pseae Elongation factor Tu tufA PA4265 tufB PA4277 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MAKEKFERNKPHVNVGTIGHVDHGKTTLTAALTKVCSDTWGGSARAFDQIDNAPEEKARGITINTSHVEYDSAVRHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLSRQVGVPYIVVFLNKADMVDDAELLELVEMEVRDLLNTYDFPGDDTPIIIGSALMALEGKDDNGIGVSAVQKLVETLDSYIPEPVRAIDQPFLMPIEDVFSISGRGTVVTGRVERGIIKVQEEVEIVGIKATTKTTCTGVEMFRKLLDEGRAGENVGILLRGTKREDVERGQVLAKPGTIKPHTKFECEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGNCELPEGVEMVMPGDNIKMVVTLIAPIAMEDGLRFAIREGGRTVGAGVVAKIIE A019D5BF8EBAB942 ppbl_pseae Alkaline phosphatase L lapA Low-molecular-weight alkaline phosphatase A Protein DING phoA phoA2 pstS PA0688 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MFKRSLIAASLSVAALVSAQAMAVTGGGASLPAELYKGSADSILPANFSYAVTGSGTGKNAFLTNNSSLFGTTGTVHYAGSDSVLSGSELTTYNSNYNGTYGPLIQIPSVATSVTVPYRKDGNTTLNLTSAQLCDAFSGAKTTWGQLLGTTDSTPIRIVYRTGSSGTTELFTRHLNSICPTRFATNSTFTNARLPAGGTLPSNWVGVAATSTVVSTVKATNGSLGYVSPDAVNINSNAEVSRVNGNLPTQANVSTALGSVAPPANAADRADPSKWVPVFTNPSAGYSIVGYTNFVFGQCYKDASVSTDVRAFINKHYGGTTTNAAVAAHGFIPLTPAWKSAIVSAFYTGTSENLAIGNTNVCNTKGRP 44F3D6BF203098F1 vgr2a_pseae Type VI secretion system spike protein VgrG2a vgrG2a PA1511 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MRQRDLKFTFVVGEGKLAFDVVEFELEEALCEPFRLNLKLASDKNAIDFRQVLDQPGTFTLWQDGRPARYVHGIVSHFTQGSSGFRRTRYELLLEPQLARLELCCNWRIFQEKSVPEILQALLKEHRVLDYEQRIYHEHLPREYCVQAGDSDHYLHDRLAFEEGLVYYFRFDEHRHTLVCSDRLYVQERIAGGPVLFSAQPEGDNPQPVLHSFRYSENVRTARQTQRDYSFKRPTYDQEHHLAGEALEHQGSSYERYDYPGRYKRSGAGRPFSESRLRGHRRDARVASVSGDDPRLIPGHAFALEGHPRADFNAWWRPVRVVHRGTQYAGQEEESADAPLGVSYDLRAELVPEDVEWRPAPLPRPRIDGPQIATVVGPAGEEIHCDEWGRVKVQFPWDREGRHDEFSTCWIRVAQNWAGADWGHMAIPRIGQEVIVDYLDGDCDQPIVTGRTYRATNRPPYALPDHKILSTIKSKEYKGSRANELRIDDTTAQISAALMSDHGASALHLGYLTHPRPEGGKPRGEGFELRTDEHGAVRAAKGLLLSTEEQLRAGAGHLDRGVVVQVLEAALKLARELGDYAGEHQGVGHDAAPQQTLQEAVRDLGHGANDESGKSNGGKPAIALSGPAGIAAATPASLTLAAGEHVDSVARQNQQVTAGQKVVINAGSDIGLFAQGGELRQITHQGPMLLQAQKNDIRLEAEQSVEVSASQQHVLVTAKEHITLMCGGAYLTLKGGNIELGMPGNFVVKAAKHSHVGPAHASTSFNAWDSTPFDDRYVLRDEATLEPLPNIAVEVIRGDGGVVKLMTDSQGRLPKQQHLAMDPVQIRILGKGSHNSDTESNT D10FFF81D8AEF356 gaca_pseae Response regulator GacA gacA Global activator PA2586 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MIKVLVVDDHDLVRTGITRMLADIEGLQVVGQADCGEDCLKLARELKPDVVLMDVKMPGIGGLEATRKLLRSQPDIKVVVVTVCEEDPFPTRLMQAGAAGYMTKGAGLEEMVQAIRQVFAGQRYISPQIAQQLALKSFQPQQHDSPFDSLSEREIQIALMIANCHKVQSISDKLCLSPKTVNTYRYRIFEKLSITSDVELALLAVRHGMVDAAS FB8D60AE0A40BA52 azur_pseae Azurin azu PA4922 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MLRKLAAVSLLSLLSAPLLAAECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTFPGHSALMKGTLTLK 9C3881D7B6D64B67 mint 9C3881D7B6D64B67 q9i5u9_pseae AAA_PrkA domain-containing protein PA0588 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSIFSHFQERFEATRQEEYSLQEYLDLCKQDKTAYASAAERLLMAIGEPELLDTSVDSRLSRIFSNKVIRRYPAFADFHGMEECIDQIVAFFRHAAQGLEEKKQILYLLGPVGGGKSSLAEKLKQLMEKVPFYAIKGSPVFESPLGLFNPDEDGAILEEDYGIPRRYLRSIMSPWATKRLNEFGGDISQFRVVKLYPSILNQIAIAKTEPGDENNQDISALVGKVDIRKLEEYPQNDADAYSYSGALCRANQGLMEFVEMFKAPIKVLHPLLTATQEGNYNSTEGLGALPYSGIILAHSNESEWHSFRNNKNNEAFIDRIYIVKVPYCLRVADEIKIYDKLLVNSSLAHAHCAPDTLKMLSQFSVLSRLKEPENSNIYSKMRVYDGENLKDTDPKAKSIQEYRDSAGVDEGMAGLSTRFAFKILSKVFNFDPHEVAANPVHLLYVLEQQIEQEQFQPETRERYLRFIKEYLAPRYVEFIGKEIQTAYLESYSEYGQNIFDRYVLYADFWIQDQEYRDPETGEILNRAALNEELEKIEKPAGISNPKDFRNEIVNFVLRARAGNNGKNPSWLSYEKLRVVIEKKMFSNTEDLLPVISFNAKASKEDQQKHNDFVKRMVERGYTEKQVRLLSEWYLRVRKSQ A362618DC1711847 htpg_pseae Chaperone protein HtpG htpG Heat shock protein HtpG High temperature protein G PA1596 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSVETQKETLGFQTEVKQLLHLMIHSLYSNKEIFLRELISNASDAADKLRFEALANPELLEGGAELKIRVSFDKEANTVTLEDNGIGMSREDVVTHLGTIAKSGTADFLKNLSGDQKKDSHLIGQFGVGFYSAFIVADKVDVYSRRAGQPASEGVHWSSKGEGEFDVATIDKPERGTRIVLHLKKGEEEFADGWRLRNVIKKYSDHIALPIELPKEFHGEEADKPAEPEWETVNRASALWTRPRAEVKDEEYQEFYKHVAHDFENPLSWSHNKVEGKLEYTSLLYVPGRAPFDLYHREAPRGLKLYVQRVFIMDQADEFLPLYLRFIKGVVDSNDLSLNVSREILQKDPVIDSMKSALTKRVLDMLEKLAKNEPEQYKTFWKNFGQVLKEGPAEDFGNKEKIAGLLRFASTGDDSGEQSVALADYIGRMKEGQDKIYYLTGESYSQVKNSPHLEVFRKKGIEVLLLTDRIDEWLMSYLPEFDGKQFVDVARGDLDLGSLDSEEDKKAQEEVAKSKEGLIERLKKVLDEQVSEVRVSHRLTDSPAILAIGEQDLGLQMRQILEASGQKVPDSKPIFEINPQHPLIEKLDAEPDEDRFGELSHILFDQAALAAGDSLKDPGAYVRRLNKLLVELSA ACD96C46206ECB55 azu-1 3 9 unspecified role unspecified role bait bait purified purified GST tag GST tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate flag tag flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged c-term range C-terminal range c-term range c-term range C-terminal range c-term range pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) physical association physical association f1d azu-2 2 9 unspecified role unspecified role prey prey purified purified GST tag GST tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role prey prey cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) 10 unspecified role unspecified role prey prey cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) 11 unspecified role unspecified role prey prey cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) 5 unspecified role unspecified role prey prey cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) 6 unspecified role unspecified role prey prey cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) association association f4a st2 azu-3 1 4 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate his tag his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range 8 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell flag tag flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association f4b azu-oprc-1 1 9 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell flag tag flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 4 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate his tag his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range physical association physical association f4b azu-oprc-2 3 9 unspecified role unspecified role bait bait purified purified GST tag GST tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role prey prey purified purified his tag his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) direct interaction direct interaction sf8b DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer. Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer. Nature communications 2017 imex curation Maderbocus R., Fields BL., Hamilton K., Luo S., Tran TH., Dietrich LEP., Tong L. ltong@columbia.edu Only protein-protein interactions imex curation in vitro In vitro pull down pull down predetermined predetermined participant predetermined Maderbocus R., Fields BL., Hamilton K., Luo S., Tran TH., Dietrich LEP., Tong L. ltong@columbia.edu Accepted 2021-JUL-22 AT 05:59 BST AT 05:59 BST by KALPANAP Nature communications 2017 Only protein-protein interactions imex curation imex curation Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer. Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer. Nature communications 2017 imex curation Maderbocus R., Fields BL., Hamilton K., Luo S., Tran TH., Dietrich LEP., Tong L. ltong@columbia.edu Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Maderbocus R., Fields BL., Hamilton K., Luo S., Tran TH., Dietrich LEP., Tong L. ltong@columbia.edu Accepted 2021-JUL-22 AT 05:59 BST AT 05:59 BST by KALPANAP Nature communications 2017 Only protein-protein interactions imex curation imex curation Inhibitors of bacterial H₂S biogenesis targeting antibiotic resistance and tolerance. Inhibitors of bacterial H₂S biogenesis targeting antibiotic resistance and tolerance. Science (New York, N.Y.) 2021 imex curation Shatalin K., Nuthanakanti A., Kaushik A., Shishov D., Peselis A., Shamovsky I., Pani B., Lechpammer M., Vasilyev N., Shatalina E., Rebatchouk D., Mironov A., Fedichev P., Serganov A., Nudler E. evgeny.nudler@nyulangone.org Only protein-protein interactions imex curation ecoli Escherichia coli (strain K12) molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by staining molecular weight estimation by staining weight by staining Shatalin K., Nuthanakanti A., Kaushik A., Shishov D., Peselis A., Shamovsky I., Pani B., Lechpammer M., Vasilyev N., Shatalina E., Rebatchouk D., Mironov A., Fedichev P., Serganov A., Nudler E. evgeny.nudler@nyulangone.org Accepted 2021-NOV-02 AT 07:12 GMT AT 07:12 GMT by ORCHARD Science (New York, N.Y.) 2021 imex curation mdcc_psef5 Malonate decarboxylase acyl carrier protein Malonate decarboxylase subunit delta PFL_5818 mdcC protein protein psef5 Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477) METLSFEFPAGQPGRGRALVGCVGSGDLEVLLEPGQPGKLSIQVQTSVNGSASRWQHLFERLFDGQTPPALLIDIHDFGATPGVVRLRLEQGFEEIGHD 2BC391BB422483FB q9i6t0_pseae mdcA PA0208 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MTTPISPPPQWSRRRQEKQRRLERVRGLADGAVLPREGLVAALEALIAPGDRVVLEGNNQKQADFLSRSLARVDPGKLHDLHMIMPSVGRPEHLDLFELGIARKLDFSFSGPQSLRIGQLLEDGLLEIGAIHTYIELYARLVVDLIPNVALVAGFVADREGNVYTGPSTEDTPALVEPTAFSDGIVIVQVNRIVDDPRDLPRVDIPASWVDFVVEADQPFYIEPLFTRDPRHIKPVHVLMAMMAIRGIYQRHNVQSLNHGIGFNTAAIELILPTYGESLGLKGKICRHWTLNPHPTLIPAIESGWVESVHCFGTELGMEGYIAQRPDVFFTGRDGSLRSNRMFCQLAGQYAVDLFIGATLQVDGDGHSSTVTRGRLAGFGGAPNMGHDPRGRRHSTPAWLDMRGEPEALLERGRKLVVQMVETFQDGGKPTFVERLDALEVARQTGMPLAPVMIYGDDVTHVLTEEGIAYLYKARSLEERQAMIAAVAGISPIGLRHDPRETQRMRREGLIALPEDLGIRRTDASRELLAAKSIAELVEWSGGLYQPPARFRSW 2E7E48DFF98CB097 q9i6a0_pseae PA0400 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSQHDQHPDAPAQAFATRVIHAGQAPDPSTGAIMPPIYANSTYIQESPGVHKGLDYGRSHNPTRWALERCVADLEGGTQAFAFASGLAAISSVLELLDAGSHIVSGNDLYGGTFRLFERVRRRSAGHRFSFVDPTDLQAFEAALTPETRMVWVETPSNPLLRLTDLRAIAQLCRARGIISVADNTFASPYIQRPLELGFDVVVHSTTKYLNGHSDVIGGIAIVGDNPDLRERLGFLQNSVGAISGPFDAFLTLRGVKTLALRMERHCSNALALAQWLERQPQVARVYYPGLASHPQHELAKRQMRGFGGMISLDLRCDLAGARRFLENVRIFSLAESLGGVESLIEHPAIMTHASIPAETRADLGIGDSLIRLSVGVEALEDLQADLAQALAKI E8F4BAC6F4BB607F q9i6s6_pseae mdcE PA0212 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSQPFASRGLAWFQALAGSLAPRPGDPASLRVADAELDGYPVRFLAVVPDPDNPFPRARQGEVGLLEGWGLAAAVDEALEADREAPRKRALLAIVDVPSQAYGRREEALGIHQALAGAVDAYARARLAGHPLIGLLVGKAMSGAFLAHGYQANRLIALHDPGVMVHAMGKAAAARITLRSVEELEALAAKVPPMAYDIDSYASLGLLWRTLPVETVEVPSTADLVRVRTCLGEALADILGGPRDLGGRLGAANREASARVRRLLREQW 5465BF4F69FECE45 q9i6s7_pseae mdcD PA0211 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MTDVARLLALRSFTELGARQRARALLDAGSFRELLDPFAGVQSPWLERQGIVPQADDGVVVARGLLDGQPAVLAAIEGAFQGGSLGEVSGAKIAGALELAAEDNRNGVPTRALLLLETGGVRLQEANLGLAAIAEIQAAIVDLQRYQPVVAVIAGPVGCFGGMSIAAGLCSYVLVTREARLGLNGPQVIEQEAGIAEYDSRDRPFIWSLTGGEQRFASGLADAYLADDLDEVRTSVLAYFAKGLPARPRCRRAEDYLRRLGDLDTAEQPDAAGVRRLYQGLGQGDAT 3888ADBDEF23CFF4 mdcd-mdce-1 2 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig 2, Table 1 mdca-mdcc-1 2 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) physical association physical association Fig 3, Table 1 mdca-mdcc-3 1 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range required to bind required to bind required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) physical association physical association Fig 4f mdca-mdcc-4 1 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified required to bind required to bind required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) physical association physical association Fig 4f mdca-mdcc-5 1 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified Q4K4F7:p.[Thr81Asp;Pro82Glu;Gly83Asp] p.[T81D;P82E;G83D] mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain G D certain certain sequence position certain certain certain sequence position certain T D certain certain sequence position certain certain certain sequence position certain P E Mon Jun 28 17:14:48 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Thr81Asp;Pro82Glu;Gly83Asp]' ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) physical association physical association Fig 4f mdca-mdcc-6 1 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified Q9I6T0:p.Phe424Ala p.F424A mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain F A Mon Jun 28 17:22:23 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe424Ala' ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) physical association physical association Fig 4f mdca-mdcc-7 1 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified Q9I6T0:p.Ile490Ala p.I490A mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain I A Mon Jun 28 17:47:59 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile490Ala' ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) physical association physical association Fig 4f mdca-mdcc-8 1 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified Q9I6T0:p.Arg521Ala p.R521A mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain R A Mon Jun 28 17:29:35 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg521Ala' ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) physical association physical association Fig 4f mdca-mdcc-9 1 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified Q9I6T0:p.Glu466Ala p.E466A mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain E A Mon Jun 28 17:46:35 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu466Ala' ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) physical association physical association Fig 4f mdca-mdcc-10 1 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified Q9I6T0:p.Arg500Ala p.R500A mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain R A Mon Jun 28 16:57:43 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg500Ala' ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) physical association physical association Fig 4f mdca-mdcc-11 1 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified Q4K4F7:p.Arg61Ala p.R61A mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain R A Mon Jun 28 17:20:33 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg61Ala' ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) physical association physical association Fig 4f mdca-mdcc-12 1 5 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified Q4K4F7:p.Pro82Ala p.P82A mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain P A Mon Jun 28 16:59:41 BST 2021 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro82Ala' ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) physical association physical association Fig 4f q9i6a0_pseae-1 3 6 weight by staining molecular weight estimation by staining weight by staining experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed purified purified ecoli Escherichia coli (strain K12) physical association physical association Supp. Fig. 9A