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/ Protein complexes of the Escherichia coli cell envelope. Protein complexes of the Escherichia coli cell envelope. J. Biol. Chem. (0021-9258) 2005 Stenberg F., Chovanec P., Maslen SL., Robinson CV., Ilag LL., von Heijne G., Daley DO. The authors state that a number of proteins of expected molecular mass were observed in a number of complexes isolated in this assay. However these proteins could not be subsequently identified by mass spectrometry and are therefore not entered as components of the complexes curated in this entry. However where such instances arise the presence of the unidentfied proteins is commented on in the complex properties annotation text. E.coli inner and outer membrane vesicles were isolated by successive sucrose gradient purification steps. The authors empirically deduced that solubilisation using n-dodecyl-beta-D-maltoside (DDM) as the most effective solubilsation agent and this was used to prepare solubilised membranes. ddaley@dbb.su.se 10-APR-2007: Contacted by JYOTI. ecoli Escherichia coli (strain K12) bn-page blue native page bn-page ms participant Identification by mass spectrometry ms participant Stenberg F., Chovanec P., Maslen SL., Robinson CV., Ilag LL., von Heijne G., Daley DO. The authors state that a number of proteins of expected molecular mass were observed in a number of complexes isolated in this assay. However these proteins could not be subsequently identified by mass spectrometry and are therefore not entered as components of the complexes curated in this entry. However where such instances arise the presence of the unidentfied proteins is commented on in the complex properties annotation text. E.coli inner and outer membrane vesicles were isolated by successive sucrose gradient purification steps. The authors empirically deduced that solubilisation using n-dodecyl-beta-D-maltoside (DDM) as the most effective solubilsation agent and this was used to prepare solubilised membranes. ddaley@dbb.su.se Accepted 2007-APR-23 by JYOTI. 10-APR-2007: Contacted by JYOTI. J. Biol. Chem. (0021-9258) 2005 epta_ecoli Phosphoethanolamine transferase EptA pmrC yjdB eptA b4114 JW5730 Polymyxin resistance protein PmrC protein protein ecoli Escherichia coli (strain K12) MLKRLLKRPSLNLLAWLLLAAFYISICLNIAFFKQVLQALPLDSLHNVLVFLSMPVVAFSVINIVLTLSSFLWLNRPLACLFILVGAAAQYFIMTYGIVIDRSMIANIIDTTPAESYALMTPQMLLTLGFSGVLAALIACWIKIKPATSRLRSVLFRGANILVSVLLILLVAALFYKDYASLFRNNKELVKSLSPSNSIVASWSWYSHQRLANLPLVRIGEDAHRNPLMQNEKRKNLTILIVGETSRAENFSLNGYPRETNPRLAKDNVVYFPNTASCGTATAVSVPCMFSDMPREHYKEELAQHQEGVLDIIQRAGINVLWNDNDGGCKGACDRVPHQNVTALNLPDQCINGECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFTPTCDTNEIQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSDHGESLGENGIYLHGLPYAIAPDSQKQVPMLLWLSEDYQKRYQVDQNCLQKQAQTQHYSQDNLFSTLLGLTGVETKYYQAADDILQTCRRVSE DIP protein P30845 original sequence version: null AA8CE79DDC2F8D10 atpl_ecoli ATP synthase subunit c Lipid-binding protein Dicyclohexylcarbodiimide-binding protein atpE papH uncE b3737 JW3715 ATP synthase F(0) sector subunit c F-type ATPase subunit c protein protein ecoli Escherichia coli (strain K12) MENLNMDLLYMAAAVMMGLAAIGAAIGIGILGGKFLEGAARQPDLIPLLRTQFFIVMGLVDAIPMIAVGLGLYVMFAVA 0F595A69D8AD1F9E bama_ecoli Outer membrane protein assembly factor BamA bamA Omp85 yaeT yzzN yzzY JW0172 b0177 protein protein ecoli Escherichia coli (strain K12) MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGDTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTIADIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAEIQQINIVGNHAFTTDELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYVTVNITEGDQYKLSGVEVSGNLAGHSAEIEQLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSMPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDAVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYAVGINGTKNDYQTYAELSVTNPYFTVDGVSLGGRLFYNDFQADDADLSDYTNKSYGTDVTLGFPINEYNSLRAGLGYVHNSLSNMQPQVAMWRYLYSMGEHPSTSDQDNSFKTDDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKVTLDTATYVPIDDDHKWVVLGRTRWGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYFPHQASNYDPDYDYECATQDGAKDLCKSDDAVGGNAMAVASLEFITPTPFISDKYANSVRTSFFWDMGTVWDTNWDSSQYSGYPDYSDPSNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW DIP protein P0A940 original sequence version: 84 DIP protein P0A940 original sequence version: 102 DIP protein P0A940 original sequence version: 103 DDCE4C6D341664EB atpf_ecoli ATP synthase subunit b atpF papF uncF b3736 JW3714 ATP synthase F(0) sector subunit b F-type ATPase subunit b ATPase subunit I protein protein ecoli Escherichia coli (strain K12) MNLNATILGQAIAFVLFVLFCMKYVWPPLMAAIEKRQKEIADGLASAERAHKDLDLAKASATDQLKKAKAEAQVIIEQANKRRSQILDEAKAEAEQERTKIVAQAQAEIEAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 51A93C8BEE9AD9DF ompa_ecoli Outer membrane protein A ompA tolG tut con Outer membrane protein II* b0957 JW0940 Outer membrane porin A Outer membrane protein 3A Outer membrane protein B Outer membrane protein d protein protein ecoli Escherichia coli (strain K12) MKKTAIAIAVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFINNNGPTHENQLGAGAFGGYQVNPYVGFEMGYDWLGRMPYKGSVENGAYKAQGVQLTAKLGYPITDDLDIYTRLGGMVWRADTKSNVYGKNHDTGVSPVFAGGVEYAITPEIATRLEYQWTNNIGDAHTIGTRPDNGMLSLGVSYRFGQGEAAPVVAPAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGMGESNPVTGNTCDNVKQRAALIDCLAPDRRVEIEVKGIKDVVTQPQA DIP protein P0A910 original sequence version: 81 DIP protein P0A910 original sequence version: 79 DIP protein P0A910 original sequence version: 61 DIP protein P0A910 original sequence version: 54 DIP protein P0A910 original sequence version: 67 DIP protein P0A910 original sequence version: 88 DIP protein P0A910 original sequence version: 93 195147734CDF8B04 cyda_ecoli Cytochrome bd-I ubiquinol oxidase subunit 1 cydA cyd-1 b0733 Cytochrome d ubiquinol oxidase subunit I Cytochrome bd-I oxidase subunit I JW0722 protein protein ecoli Escherichia coli (strain K12) MLDIVELSRLQFALTAMYHFLFVPLTLGMAFLLAIMETVYVLSGKQIYKDMTKFWGKLFGINFALGVATGLTMEFQFGTNWSYYSHYVGDIFGAPLAIEGLMAFFLESTFVGLFFFGWDRLGKVQHMCVTWLVALGSNLSALWILVANGWMQNPIASDFNFETMRMEMVSFSELVLNPVAQVKFVHTVASGYVTGAMFILGISAWYMLKGRDFAFAKRSFAIAASFGMAAVLSVIVLGDESGYEMGDVQKTKLAAIEAEWETQPAPAAFTLFGIPDQEEETNKFAIQIPYALGIIATRSVDTPVIGLKELMVQHEERIRNGMKAYSLLEQLRSGSTDQAVRDQFNSMKKDLGYGLLLKRYTPNVADATEAQIQQATKDSIPRVAPLYFAFRIMVACGFLLLAIIALSFWSVIRNRIGEKKWLLRAALYGIPLPWIAVEAGWFVAEYGRQPWAIGEVLPTAVANSSLTAGDLIFSMVLICGLYTLFLVAELFLMFKFARLGPSSLKTGRYHFEQSSTTTQPAR E757442068BCFCFE lep_ecoli Signal peptidase I lepB b2568 JW2552 Leader peptidase I protein protein ecoli Escherichia coli (strain K12) MANMFALILVIATLVTGILWCVDKFFFAPKRRERQAAAQAAAGDSLDKATLKKVAPKPGWLETGASVFPVLAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPIYQKTLIETGHPKRGDIVVFKYPEDPKLDYIKRAVGLPGDKVTYDPVSKELTIQPGCSSGQACENALPVTYSNVEPSDFVQTFSRRNGGEATSGFFEVPKNETKENGIRLSERKETLGDVTHRILTVPIAQDQVGMYYQQPGQQLATWIVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGRATAIWMSFDKQEGEWPTGLRLSRIGGIH 9419710D7212E660 nuog_ecoli NADH-quinone oxidoreductase subunit G NADH dehydrogenase I subunit G NDH-1 subunit G NUO7 nuoG b2283 JW2278 protein protein ecoli Escherichia coli (strain K12) MATIHVDGKEYEVNGADNLLEACLSLGLDIPYFCWHPALGSVGACRQCAVKQYQNAEDTRGRLVMSCMTPASDGTFISIDDEEAKQFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSFRRYRFTKRTHRNQDLGPFISHEMNRCIACYRCVRYYKDYADGTDLGVYGAHDNVYFGRPEDGTLESEFSGNLVEICPTGVFTDKTHSERYNRKWDMQFAPSICQQCSIGCNISPGERYGELRRIENRYNGTVNHYFLCDRGRFGYGYVNLKDRPRQPVQRRGDDFITLNAEQAMQGAADILRQSKKVIGIGSPRASVESNFALRELVGEENFYTGIAHGEQERLQLALKVLREGGIYTPALREIESYDAVLVLGEDVTQTGARVALAVRQAVKGKAREMAAAQKVADWQIAAILNIGQRAKHPLFVTNVDDTRLDDIAAWTYRAPVEDQARLGFAIAHALDNSAPAVDGIEPELQSKIDVIVQALAGAKKPLIISGTNAGSLEVIQAAANVAKALKGRGADVGITMIARSVNSMGLGIMGGGSLEEALTELETGRADAVVVLENDLHRHASAIRVNAALAKAPLVMVVDHQRTAIMENAHLVLSAASFAESDGTVINNEGRAQRFFQVYDPAYYDSKTVMLESWRWLHSLHSTLLSREVDWTQLDHVIDAVVAKIPELAGIKDAAPDATFRIRGQKLAREPHRYSGRTAMRANISVHEPRQPQDIDTMFTFSMEGNNQPTAHRSQVPFAWAPGWNSPQAWNKFQDEVGGKLRFGDPGVRLFETSENGLDYFTSVPARFQPQDGKWRIAPYYHLFGSDELSQRAPVFQSRMPQPYIKLNPADAAKLGVNAGTRVSFSYDGNTVTLPVEIAEGLTAGQVGLPMGMSGIAPVLAGAHLEDLKEAQQ DIP protein P33602 original sequence version: 104 DIP protein P33602 original sequence version: null 7B8626E19709D540 fadl_ecoli Long-chain fatty acid transport protein Outer membrane FadL protein fadL ttr b2344 JW2341 Outer membrane flp protein protein protein ecoli Escherichia coli (strain K12) MSQKTLFTKSALAVAVALISTQAWSAGFQLNEFSSSGLGRAYSGEGAIADDAGNVSRNPALITMFDRPTFSAGAVYIDPDVNISGTSPSGRSLKADNIAPTAWVPNMHFVAPINDQFGWGASITSNYGLATEFNDTYAGGSVGGTTDLETMNLNLSGAYRLNNAWSFGLGFNAVYARAKIERFAGDLGQLVAGQIMQSPAGQTQQGQALAATANGIDSNTKIAHLNGNQWGFGWNAGILYELDKNNRYALTYRSEVKIDFKGNYSSDLNRAFNNYGLPIPTATGGATQSGYLTLNLPEMWEVSGYNRVDPQWAIHYSLAYTSWSQFQQLKATSTSGDTLFQKHEGFKDAYRIALGTTYYYDDNWTFRTGIAFDDSPVPAQNRSISIPDQDRFWLSAGTTYAFNKDASVDVGVSYMHGQSVKINEGPYQFESEGKAWLFGTNFNYAF 9B50C55D82CDB085 slp_ecoli Outer membrane protein Slp slp b3506 JW3474 protein protein ecoli Escherichia coli (strain K12) MNMTKGALILSLSFLLAACSSIPQNIKGNNQPDIQKSFVAVHNQPGLYVGQQARFGGKVINVINGKTDTLLEISVLPLDSYAKPDIEANYQGRLLARQSGFLDPVNYRNHFVTILGTIQGEQPGFINKVPYNFLEVNMQGIQVWHLREVVNTTYNLWDYGYGAFWPEPGWGAPYYTNAVSQVTPELVK B2CDBC40E05ADB30 mscs_ecoli Small-conductance mechanosensitive channel yggB mscS b2924 JW2891 protein protein ecoli Escherichia coli (strain K12) MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRKIDATVADFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSREPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVWSNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRVKEDKAA FF00AD64F795E9FE bamc_ecoli Outer membrane protein assembly factor BamC bamC dapX nlpB JW2462 b2477 protein protein ecoli Escherichia coli (strain K12) MAYSVQKSRLAKVAGVSLVLLLAACSSDSRYKRQVSGDEAYLEAAPLAELHAPAGMILPVTSGDYAIPVTNGSGAVGKALDIRPPAQPLALVSGARTQFTGDTASLLVENGRGNTLWPQVVSVLQAKNYTITQRDDAGQTLTTDWVQWNRLDEDEQYRGRYQISVKPQGYQQAVTVKLLNLEQAGKPVADAASMQRYSTEMMNVISAGLDKSATDAANAAQNRASTTMDVQSAADDTGLPMLVVRGPFNVVWQRLPAALEKVGMKVTDSTRSQGNMAVTYKPLSDSDWQELGASDPGLASGDYKLQVGDLDNRSSLQFIDPKGHTLTQSQNDALVAVFQAAFSK DIP protein P0A903 original sequence version: 95 DIP protein P0A903 original sequence version: 96 49991F277D9D923C acrb_ecoli Multidrug efflux pump subunit AcrB acrB acrE b0462 JW0451 AcrAB-TolC multidrug efflux pump subunit AcrB Acridine resistance protein B protein protein ecoli Escherichia coli (strain K12) MPNFFIDRPIFAWVIAIIIMLAGGLAILKLPVAQYPTIAPPAVTISASYPGADAKTVQDTVTQVIEQNMNGIDNLMYMSSNSDSTGTVQITLTFESGTDADIAQVQVQNKLQLAMPLLPQEVQQQGVSVEKSSSSFLMVVGVINTDGTMTQEDISDYVAANMKDAISRTSGVGDVQLFGSQYAMRIWMNPNELNKFQLTPVDVITAIKAQNAQVAAGQLGGTPPVKGQQLNASIIAQTRLTSTEEFGKILLKVNQDGSRVLLRDVAKIELGGENYDIIAEFNGQPASGLGIKLATGANALDTAAAIRAELAKMEPFFPSGLKIVYPYDTTPFVKISIHEVVKTLVEAIILVFLVMYLFLQNFRATLIPTIAVPVVLLGTFAVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVMAEEGLPPKEATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGSTGAIYRQFSITIVSAMALSVLVALILTPALCATMLKPIAKGDHGEGKKGFFGWFNRMFEKSTHHYTDSVGGILRSTGRYLVLYLIIVVGMAYLFVRLPSSFLPDEDQGVFMTMVQLPAGATQERTQKVLNEVTHYYLTKEKNNVESVFAVNGFGFAGRGQNTGIAFVSLKDWADRPGEENKVEAITMRATRAFSQIKDAMVFAFNLPAIVELGTATGFDFELIDQAGLGHEKLTQARNQLLAEAAKHPDMLTSVRPNGLEDTPQFKIDIDQEKAQALGVSINDINTTLGAAWGGSYVNDFIDRGRVKKVYVMSEAKYRMLPDDIGDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKSTGEAMELMEQLASKLPTGVGYDWTGMSYQERLSGNQAPSLYAISLIVVFLCLAALYESWSIPFSVMLVVPLGVIGALLAATFRGLTNDVYFQVGLLTTIGLSAKNAILIVEFAKDLMDKEGKGLIEATLDAVRMRLRPILMTSLAFILGVMPLVISTGAGSGAQNAVGTGVMGGMVTATVLAIFFVPVFFVVVRRRFSRKNEDIEHSHTVDHH DIP protein P31224 original sequence version: 128 DIP protein P31224 original sequence version: 73 DIP protein P31224 original sequence version: 136 DIP protein P31224 original sequence version: 112 DIP protein P31224 original sequence version: 126 DIP protein P31224 original sequence version: null 19670E3C4CC29055 ompf_ecoli Outer membrane porin F ompF cmlB tolF coa cry Porin OmpF Outer membrane protein 1A Outer membrane protein IA Outer membrane protein B b0929 JW0912 Outer membrane protein F protein protein ecoli Escherichia coli (strain K12) MMKRNILAVIVPALLVAGTANAAEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGATYYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF 3F0974D96DB65464 3F0974D96DB65464 lpp_ecoli Major outer membrane lipoprotein Lpp lpp mlpA mulI b1677 JW1667 Braun lipoprotein Murein-lipoprotein protein protein ecoli Escherichia coli (strain K12) MKATKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK DIP protein P69776 original sequence version: 52 19F41D5251913C93 actp_ecoli Cation/acetate symporter ActP yjcG Acetate transporter ActP Acetate permease actP b4067 JW4028 protein protein ecoli Escherichia coli (strain K12) MKRVLTALAATLPFAANAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFSEAMAVHPKGVDIMKPGGLVKDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPEYKDAAGHLIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFKKGATEREELRVSKITVLILGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMMGGWLGLITAVVLMILGPTIWVQILGHEKAIFPYEYPALFSITVAFLGIWFFSATDNSAEGARERELFRAQFIRSQTGFGVEQGRAH DIP protein P32705 original sequence version: 83 DIP protein P32705 original sequence version: null E7E116FB919D0FFD ppid_ecoli Periplasmic chaperone PpiD ybaU ppiD b0441 JW0431 Periplasmic folding chaperone protein protein ecoli Escherichia coli (strain K12) MMDSLRTAANSLVLKIIFGIIIVSFILTGVSGYLIGGGNNYAAKVNDQEISRGQFENAFNSERNRMQQQLGDQYSELAANEGYMKTLRQQVLNRLIDEALLDQYARELKLGISDEQVKQAIFATPAFQVDGKFDNSRYNGILNQMGMTADQYAQALRNQLTTQQLINGVAGTDFMLKGETDELAALVAQQRVVREATIDVNALAAKQPVTEQEIASYYEQNKNNFMTPEQFRVSYIKLDAATMQQPVSDADIQSYYDQHQDQFTQPQRTRYSIIQTKTEDEAKAVLDELNKGGDFAALAKEKSADIISARNGGDMGWLEDATIPDELKNAGLKEKGQLSGVIKSSVGFLIVRLDDIQPAKVKSLDEVRDDIAAKVKHEKALDAYYALQQKVSDAASNDTESLAGAEQAAGVKATQTGWFSKDNLPEELNFKPVADAIFNGGLVGENGAPGINSDIITVDGDRAFVLRISEHKPEAVKPLADVQEQVKALVQHNKAEQQAKVDAEKLLVDLKAGKGAEAMQAAGLKFGEPKTLSRSGRDPISQAAFALPLPAKDKPSYGMATDMQGNVVLLALDEVKQGSMPEDQKKAMVQGITQNNAQIVFEALMSNLRKEAKIKIGDALEQQ 0F646F687114A387 atpb_ecoli ATP synthase subunit beta atpD papB uncD b3732 JW3710 ATP synthase F1 sector subunit beta F-ATPase subunit beta protein protein ecoli Escherichia coli (strain K12) MATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNERLVLEVQQQLGGGIVRTIAMGSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLSQPFFVAEVFTGSPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEEAVEKAKKL DIP protein P0ABB4 original sequence version: 61 18DB33154B1AE6FE sdha_ecoli Succinate dehydrogenase flavoprotein subunit sdhA b0723 JW0713 protein protein ecoli Escherichia coli (strain K12) MKLPVREFDAVVIGAGGAGMRAALQISQSGQTCALLSKVFPTRSHTVSAQGGITVALGNTHEDNWEWHMYDTVKGSDYIGDQDAIEYMCKTGPEAILELEHMGLPFSRLDDGRIYQRPFGGQSKNFGGEQAARTAAAADRTGHALLHTLYQQNLKNHTTIFSEWYALDLVKNQDGAVVGCTALCIETGEVVYFKARATVLATGGAGRIYQSTTNAHINTGDGVGMAIRAGVPVQDMEMWQFHPTGIAGAGVLVTEGCRGEGGYLLNKHGERFMERYAPNAKDLAGRDVVARSIMIEIREGRGCDGPWGPHAKLKLDHLGKEVLESRLPGILELSRTFAHVDPVKEPIPVIPTCHYMMGGIPTKVTGQALTVNEKGEDVVVPGLFAVGEIACVSVHGANRLGGNSLLDLVVFGRAAGLHLQESIAEQGALRDASESDVEASLDRLNRWNNNRNGEDPVAIRKALQECMQHNFSVFREGDAMAKGLEQLKVIRERLKNARLDDTSSEFNTQRVECLELDNLMETAYATAVSANFRTESRGAHSRFDFPDRDDENWLCHSLYLPESESMTRRSVNMEPKLRPAFPPKIRTY 837F9A63991B6CE8 putp_ecoli Sodium/proline symporter putP b1015 JW1001 Propionate transporter Proline permease protein protein ecoli Escherichia coli (strain K12) MAISTPMLVTFCVYIFGMILIGFIAWRSTKNFDDYILGGRSLGPFVTALSAGASDMSGWLLMGLPGAVFLSGISESWIAIGLTLGAWINWKLVAGRLRVHTEYNNNALTLPDYFTGRFEDKSRILRIISALVILLFFTIYCASGIVAGARLFESTFGMSYETALWAGAAATILYTFIGGFLAVSWTDTVQASLMIFALILTPVIVIISVGGFGDSLEVIKQKSIENVDMLKGLNFVAIISLMGWGLGYFGQPHILARFMAADSHHSIVHARRISMTWMILCLAGAVAVGFFGIAYFNDHPALAGAVNQNAERVFIELAQILFNPWIAGILLSAILAAVMSTLSCQLLVCSSAITEDLYKAFLRKHASQKELVWVGRVMVLVVALVAIALAANPENRVLGLVSYAWAGFGAAFGPVVLFSVMWSRMTRNGALAGMIIGALTVIVWKQFGWLGLYEIIPGFIFGSIGIVVFSLLGKAPSAAMQKRFAEADAHYHSAPPSRLQES 37AE923C33186356 yhcb_ecoli Inner membrane protein YhcB yhcB b3233 JW5539 protein protein ecoli Escherichia coli (strain K12) MTWEYALIGLVVGIIIGAVAMRFGNRKLRQQQALQYELEKNKAELDEYREELVSHFARSAELLDTMAHDYRQLYQHMAKSSSSLLPELSAEANPFRNRLAESEASNDQAPVQMPRDYSEGASGLLRTGAKRD 6A57A58B5FD1C171 cydb_ecoli Cytochrome bd-I ubiquinol oxidase subunit 2 cydB cyd-2 b0734 JW0723 Cytochrome d ubiquinol oxidase subunit II Cytochrome bd-I oxidase subunit II protein protein ecoli Escherichia coli (strain K12) MIDYEVLRFIWWLLVGVLLIGFAVTDGFDMGVGMLTRFLGRNDTERRIMINSIAPHWDGNQVWLITAGGALFAAWPMVYAAAFSGFYVAMILVLASLFFRPVGFDYRSKIEETRWRNMWDWGIFIGSFVPPLVIGVAFGNLLQGVPFNVDEYLRLYYTGNFFQLLNPFGLLAGVVSVGMIITQGATYLQMRTVGELHLRTRATAQVAALVTLVCFALAGVWVMYGIDGYVVKSTMDHYAASNPLNKEVVREAGAWLVNFNNTPILWAIPALGVVLPLLTILTARMDKAAWAFVFSSLTLACIILTAGIAMFPFVMPSSTMMNASLTMWDATSSQLTLNVMTWVAVVLVPIILLYTAWCYWKMFGRITKEDIERNTHSLY A3775AC95F713D0C zipa_ecoli Cell division protein ZipA zipA FtsZ interacting protein A JW2404 b2412 protein protein ecoli Escherichia coli (strain K12) MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPHPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGPALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVVLDDQRRMMTPQKLREYQDIIREVKDANA DIP protein P77173 original sequence version: 111 A20F119A153A782B atpg_ecoli ATP synthase gamma chain atpG papC uncG b3733 ATP synthase F1 sector gamma subunit JW3711 F-ATPase gamma subunit protein protein ecoli Escherichia coli (strain K12) MAGAKEIRSKIASVQNTQKITKAMEMVAASKMRKSQDRMAASRPYAETMRKVIGHLAHGNLEYKHPYLEDRDVKRVGYLVVSTDRGLCGGLNINLFKKLLAEMKTWTDKGVQCDLAMIGSKGVSFFNSVGGNVVAQVTGMGDNPSLSELIGPVKVMLQAYDEGRLDKLYIVSNKFINTMSQVPTISQLLPLPASDDDDLKHKSWDYLYEPDPKALLDTLLRRYVESQVYQGVVENLASEQAARMVAMKAATDNGGSLIKELQLVYNKARQASITQELTEIVSGAAAV DIP protein P0ABA6 original sequence version: 46 DIP protein P0ABA6 original sequence version: 56 2417A4B8FBDB8EF8 sdhb_ecoli Succinate dehydrogenase iron-sulfur subunit sdhB b0724 JW0714 protein protein ecoli Escherichia coli (strain K12) MRLEFSIYRYNPDVDDAPRMQDYTLEADEGRDMMLLDALIQLKEKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRNA 226F60C55F5AC35A seca_ecoli Protein translocase subunit SecA secA azi pea prlD b0098 JW0096 protein protein ecoli Escherichia coli (strain K12) MLIKLLTKVFGSRNDRTLRRMRKVVNIINAMEPEMEKLSDEELKGKTAEFRARLEKGEVLENLIPEAFAVVREASKRVFGMRHFDVQLLGGMVLNERCIAEMRTGEGKTLTATLPAYLNALTGKGVHVVTVNDYLAQRDAENNRPLFEFLGLTVGINLPGMPAPAKREAYAADITYGTNNEYGFDYLRDNMAFSPEERVQRKLHYALVDEVDSILIDEARTPLIISGPAEDSSEMYKRVNKIIPHLIRQEKEDSETFQGEGHFSVDEKSRQVNLTERGLVLIEELLVKEGIMDEGESLYSPANIMLMHHVTAALRAHALFTRDVDYIVKDGEVIIVDEHTGRTMQGRRWSDGLHQAVEAKEGVQIQNENQTLASITFQNYFRLYEKLAGMTGTADTEAFEFSSIYKLDTVVVPTNRPMIRKDLPDLVYMTEAEKIQAIIEDIKERTAKGQPVLVGTISIEKSELVSNELTKAGIKHNVLNAKFHANEAAIVAQAGYPAAVTIATNMAGRGTDIVLGGSWQAEVAALENPTAEQIEKIKADWQVRHDAVLEAGGLHIIGTERHESRRIDNQLRGRSGRQGDAGSSRFYLSMEDALMRIFASDRVSGMMRKLGMKPGEAIEHPWVTKAIANAQRKVESRNFDIRKQLLEYDDVANDQRRAIYSQRNELLDVSDVSETINSIREDVFKATIDAYIPPQSLEEMWDIPGLQERLKNDFDLDLPIAEWLDKEPELHEETLRERILAQSIEVYQRKEEVVGAEMMRHFEKGVMLQTLDSLWKEHLAAMDYLRQGIHLRGYAQKDPKQEYKRESFSMFAAMLESLKYEVISTLSKVQVRMPEEVEELEQQRRMEAERLAQMQQLSHQDDDSAAAAALAAQTGERKVGRNDPCPCGSGKKYKQCHGRLQ DIP protein P10408 original sequence version: 150 DIP protein P10408 original sequence version: 130 DIP protein P10408 original sequence version: 105 DIP protein P10408 original sequence version: 107 DIP protein P10408 original sequence version: 125 DIP protein P10408 original sequence version: 140 DIP protein P10408 original sequence version: null 683D66DD4305DBC2 acra_ecoli Multidrug efflux pump subunit AcrA acrA lir mtcA b0463 JW0452 AcrAB-TolC multidrug efflux pump subunit AcrA Acridine resistance protein A protein protein ecoli Escherichia coli (strain K12) MNKNRGFTPLAVVLMLSGSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTADNNQQAASGAQPEQSKS 5B81DD5BC2B0A077 5B81DD5BC2B0A077 mdte_ecoli Multidrug resistance protein MdtE yhiU mdtE b3513 JW3481 protein protein ecoli Escherichia coli (strain K12) MNRRRKLLIPLLFCGAMLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQENASTESKQ 2C825B6CDE15C70F 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 yajc_ecoli Sec translocon accessory complex subunit YajC yajC b0407 JW0397 protein protein ecoli Escherichia coli (strain K12) MSFFISDAVAATGAPAQGSPMSLILMLVVFGLIFYFMILRPQQKRTKEHKKLMDSIAKGDEVLTNGGLVGRVTKVAENGYIAIALNDTTEVVIKRDFVAAVLPKGTMKAL DIP protein P0ADZ7 original sequence version: 19 8E90AF51F0205306 wzzb_ecoli Chain length determinant protein wzzB cld rol wzz b2027 JW5836 Polysaccharide antigen chain regulator protein protein ecoli Escherichia coli (strain K12) MRVENNNVSGQNHDPEQIDLIDLLVQLWRGKMTIIISVIVAIALAIGYLAVAKEKWTSTAIITQPDVGQIAGYNNAMNVIYGQAAPKVSDLQETLIGRFSSAFSALAETLDNQEEREKLTIEPSVKNQQLPLTVSYVGQTAEGAQMKLAQYIQQVDDKVNQELEKDLKDNIALGRKNLQDSLRTQEVVAQEQKDLRIRQIQEALQYANQAQVTKPQIQQTGEDITQDTLFLLGSEALESMIKHEATRPLVFSPNYYQTRQNLLDIESLKVDDLDIHAYRYVMKPMLPIRRDSPKKAITLILAVLLGGMVGAGIVLGRNALRNYNAK 9D4DA2A9E5E7E8F8 atpa_ecoli ATP synthase subunit alpha atpA papA uncA b3734 JW3712 ATP synthase F1 sector subunit alpha F-ATPase subunit alpha protein protein ecoli Escherichia coli (strain K12) MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALAIDAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNAEYVEAFTKGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHAPLMQEINQTGGYNDEIEGKLKGILDSFKATQSW DIP protein P0ABB0 original sequence version: 49 DIP protein P0ABB0 original sequence version: 64 DD1F3859375E9103 hemx_ecoli Protein HemX hemX b3803 JW3775 ORF X protein protein ecoli Escherichia coli (strain K12) MTEQEKTSAVVEETREAVDTTSQPVATEKKSKNNTALILSAVAIAIALAAGIGLYGWGKQQAVNQTATSDALANQLTALQKAQESQKAELEGIIKQQAAQLKQANRQQETLAKQLDEVQQKVATISGSDAKTWLLAQADFLVKLAGRKLWSDQDVTTAAALLKSADASLADMNDPSLITVRRAITDDIASLSAVSQVDYDGIILKLNQLSNQVDNLRLADNDSDGSPMDSDGEELSSSISEWRINLQKSWQNFMDNFITIRRRDDTAVPLLAPNQDIYLRENIRSRLLVAAQAVPRHQEETYRQALENVSTWVRAYYDTDDATTKAFLDEVDQLSQQNISMDLPETLQSQAMLEKLMQTRVRNLLAQPAAGTTEAKPAPAPQADTPAAAPQGE 9D272C6401D0E354 nuocd_ecoli NADH-quinone oxidoreductase subunit C/D nuoC nuoCD nuoD b2286 NADH dehydrogenase I subunit C/D NDH-1 subunit C/D NUO3/NUO4 JW5375 protein protein ecoli Escherichia coli (strain K12) MTDLTAQEPAWQTRDHLDDPVIGELRNRFGPDAFTVQATRTGVPVVWIKREQLLEVGDFLKKLPKPYVMLFDLHGMDERLRTHREGLPAADFSVFYHLISIDRNRDIMLKVALAENDLHVPTFTKLFPNANWYERETWDLFGITFDGHPNLRRIMMPQTWKGHPLRKDYPARATEFSPFELTKAKQDLEMEALTFKPEEWGMKRGTENEDFMFLNLGPNHPSAHGAFRIVLQLDGEEIVDCVPDIGYHHRGAEKMGERQSWHSYIPYTDRIEYLGGCVNEMPYVLAVEKLAGITVPDRVNVIRVMLSELFRINSHLLYISTFIQDVGAMTPVFFAFTDRQKIYDLVEAITGFRMHPAWFRIGGVAHDLPRGWDRLLREFLDWMPKRLASYEKAALQNTILKGRSQGVAAYGAKEALEWGTTGAGLRATGIDFDVRKARPYSGYENFDFEIPVGGGVSDCYTRVMLKVEELRQSLRILEQCLNNMPEGPFKADHPLTTPPPKERTLQHIETLITHFLQVSWGPVMPANESFQMIEATKGINSYYLTSDGSTMSYRTRVRTPSFAHLQQIPAAIRGSLVSDLIVYLGSIDFVMSDVDR DIP protein P33599 original sequence version: null 5E5EB64FE2D70FDF ydga_ecoli Protein YdgA ydgA b1614 JW1606 protein protein ecoli Escherichia coli (strain K12) MNKSLVAVGVIVALGVVWTGGAWYTGKKIETHLEDMVAQANAQLKLTAPESNLEVSYQNYHRGVFSSQLQLLVKPIAGKENPWIKSGQSVIFNESVDHGPFPLAQLKKLNLIPSMASIQTTLVNNEVSKPLFDMAKGETPFEINSRIGYSGDSSSDISLKPLNYEQKDEKVAFSGGEFQLNADRDGKAISLSGEAQSGRIDAVNEYNQKVQLTFNNLKTDGSSTLASFGERVGNQKLSLEKMTISVEGKELALLEGMEISGKSDLVNDGKTINSQLDYSLNSLKVQNQDLGSGKLTLKVGQIDGEAWHQFSQQYNAQTQALLAQPEIANNPELYQEKVTEAFFSALPLMLKGDPVITIAPLSWKNSQGESALNLSLFLKDPATTKEAPQTLAQEVDRSVKSLDAKLTIPVDMATEFMTQVAKLEGYQEDQAKKLAKQQVEGASAMGQMFRLTTLQDNTITTSLQYANGQITLNGQKMSLEDFVGMFAMPALNVPAVPAIPQQ DIP protein P77804 original sequence version: null D061576FA5DBAC4C mdtf_ecoli Multidrug resistance protein MdtF mdtF b3514 yhiV JW3482 protein protein ecoli Escherichia coli (strain K12) MANYFIDRPVFAWVLAIIMMLAGGLAIMNLPVAQYPQIAPPTITVSATYPGADAQTVEDSVTQVIEQNMNGLDGLMYMSSTSDAAGNASITLTFETGTSPDIAQVQVQNKLQLAMPSLPEAVQQQGISVDKSSSNILMVAAFISDNGSLNQYDIADYVASNIKDPLSRTAGVGSVQLFGSEYAMRIWLDPQKLNKYNLVPSDVISQIKVQNNQISGGQLGGMPQAADQQLNASIIVQTRLQTPEEFGKILLKVQQDGSQVLLRDVARVELGAEDYSTVARYNGKPAAGIAIKLAAGANALDTSRAVKEELNRLSAYFPASLKTVYPYDTTPFIEISIQEVFKTLVEAIILVFLVMYLFLQNFRATIIPTIAVPVVILGTFAILSAVGFTINTLTMFGMVLAIGLLVDDAIVVVENVERVIAEDKLPPKEATHKSMGQIQRALVGIAVVLSAVFMPMAFMSGATGEIYRQFSITLISSMLLSVFVAMSLTPALCATILKAAPEGGHKPNALFARFNTLFEKSTQHYTDSTRSLLRCTGRYMVVYLLICAGMAVLFLRTPTSFLPEEDQGVFMTTAQLPSGATMVNTTKVLQQVTDYYLTKEKDNVQSVFTVGGFGFSGQGQNNGLAFISLKPWSERVGEENSVTAIIQRAMIALSSINKAVVFPFNLPAVAELGTASGFDMELLDNGNLGHEKLTQARNELLSLAAQSPNQVTGVRPNGLEDTPMFKVNVNAAKAEAMGVALSDINQTISTAFGSSYVNDFLNQGRVKKVYVQAGTPFRMLPDNINQWYVRNASGTMAPLSAYSSTEWTYGSPRLERYNGIPSMEILGEAAAGKSTGDAMKFMADLVAKLPAGVGYSWTGLSYQEALSSNQAPALYAISLVVVFLALAALYESWSIPFSVMLVVPLGVVGALLATDLRGLSNDVYFQVGLLTTIGLSAKNAILIVEFAVEMMQKEGKTPIEAIIEAARMRLRPILMTSLAFILGVLPLVISHGAGSGAQNAVGTGVMGGMFAATVLAIYFVPVFFVVVEHLFARFKKA 3B67502160F51724 yagu_ecoli Inner membrane protein YagU yagU b0287 JW0281 protein protein ecoli Escherichia coli (strain K12) MNIFEQTPPNRRRYGLAAFIGLIAGVVSAFVKWGAEVPLPPRSPVDMFNAACGPESLIRAAGQIDCSRNFLNPPYIFLRDWLGLTDPNAAVYTFAGHVFNWVGVTHIIFSIVFAVGYCVVAEVFPKIKLWQGLLAGALAQLFVHMISFPLMGLTPPLFDLPWYENVSEIFGHLVWFWSIEIIRRDLRNRITHEPDPEIPLGSNR 57EA63ED66B2E6C8 lamb_ecoli Maltoporin lamB malB Maltose-inducible porin b4036 JW3996 Maltose outer membrane channel Phage lambda receptor protein protein protein ecoli Escherichia coli (strain K12) MMITLRKLPLAVAVAAGVMSAQAMAVDFHGYARSGIGWTGSGGEQQCFQTTGAQSKYRLGNECETYAELKLGQEVWKEGDKSFYFDTNVAYSVAQQNDWEATDPAFREANVQGKNLIEWLPGSTIWAGKRFYQRHDVHMIDFYYWDISGPGAGLENIDVGFGKLSLAATRSSEAGGSSSFASNNIYDYTNETANDVFDVRLAQMEINPGGTLELGVDYGRANLRDNYRLVDGASKDGWLFTAEHTQSVLKGFNKFVVQYATDSMTSQGKGLSQGSGVAFDNEKFAYNINNNGHMLRILDHGAISMGDNWDMMYVGMYQDINWDNDNGTKWWTVGIRPMYKWTPIMSTVMEIGYDNVESQRTGDKNNQYKITLAQQWQAGDSIWSRPAIRVFATYAKWDEKWGYDYTGNADNNANFGKAVPADFNGGSFGRGDSDEWTFGAQMEIWW DIP protein P02943 original sequence version: 138 B2D4E4F120DA494E bamd_eco57 Outer membrane protein assembly factor BamD bamD yfiO ECs3458 Z3889 protein protein eco57 Escherichia coli O157:H7 MTRMKYLVAAATLSLFLAGCSGSKEEVPDNPPNEIYATAQQKLQDGNWRQAITQLEALDNRYPFGPYSQQVQLDLIYAYYKNADLPLAQAAIDRFIRLNPTHPNIDYVMYMRGLTNMALDDSALQGFFGVDRSDRDPQHARAAFSDFSKLVRGYPNSQYTTDATKRLVFLKDRLAKYEYSVAEYYTERGAWVAVVNRVEGMLRDYPDTQATRDALPLMENAYRQMQMNAQAEKVAKIIAANSSNT 91D0A25E69248C49 sdha-sdhb-sdhc 1 26 unspecified role unspecified role neutral component neutral component 20 unspecified role unspecified role neutral component neutral component physical association physical association Figure 3A From the SDS gel, we could identify the 66-kDa flavoprotein subunit (SdhA) and the 26-kDa iron-sulfur protein (SdhB) (Fig. 3A). The SdhA protein was judged to be 66 kDa and SdhB protein 26 kDa. Two other unidentified proteins that correspond in molecular mass to that predicted for SdhC (14 kDa) and SdhD (15 kDa) were also detected in the same channel. The authors concluded that the succinate dehydrogenase complex was complete (consisting of SdhA, SdhB, SdhC and SdhD proteins). cyda-cydb-yhcb 1 22 unspecified role unspecified role neutral component neutral component 7 unspecified role unspecified role neutral component neutral component 23 unspecified role unspecified role neutral component neutral component physical association physical association Figure 3B This complex is reported to be a heterodimer, CydAB, with a molecular mass of 100kDa (38). Unexpectedly, be identified CydA (58 kDa) and CydB (42 kDa) along with third proteibn, YhcB (15 kDa) The complex had an estimated molecular mass of approximately 118 kDa. Further studies by the author indicated this to be spurious interactions. nuocd-nuog 1 9 unspecified role unspecified role neutral component neutral component 35 unspecified role unspecified role neutral component neutral component physical association physical association Figure 2A A 404-kDa subcomplex contained the NuoCD protein and a 135-kDa complex contained the 90-kDa NuoG subunit The 404-kDa subcomplex contained the NuoCD protein and a 135-kDa complex contained the 90-kDa NuoG subunit I was unsure which GO:term to use either GO:0045280 (Complex that possesses NADH dehydrogenase (ubiquinone) activity, as in, but not restricted to, the taxon Bacteria) or GO:0030966 (Complex that possesses NADH dehydrogenase (quinone) activity, as in, but not restricted to, the taxon Bacteria) atpa-atpe-atpf 1 5 unspecified role unspecified role neutral component neutral component 3 unspecified role unspecified role neutral component neutral component 33 unspecified role unspecified role neutral component neutral component 19 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component physical association physical association Figure 3A The accession number given in the text is for protein subunit atpE is incorrect. The correct accession number was obtained from UniProt. We were able to identify subunit c (11 kDa), subunit b (18 kDa), the subunit (54 kDa), the subunit (51 kDa), and the subunit (29 kDa) (Fig. 3A). The complex was estimated to have a molecualr mass of 439kDa. We were able to identify subunit c (11 kDa), subunit b (18 kDa), the alpha-subunit (54 kDa), the beta-subunit(51 kDa), and the gamma-subunit (29 kDa) (Fig. 3A). Other protein spots were detected that corresponded in molecular mass to subunit a (30 kDa), the theta-subunit (19 kDa), and the epsilon-subunit (15 kDa), and we conclude that the F1-F0-ATP synthase is intact. hemx-hemx 1 34 unspecified role unspecified role neutral component neutral component physical association physical association Figure 2A Supplemental Figure 2 we conclude that HemX exists as a homo-oligomer, possibly a homopentamer. HemX exists as a homo-oligomer, possibly a homopentamer. HemX was detected as a 208kDa complex. ppid-ppid 1 18 unspecified role unspecified role neutral component neutral component physical association physical association Figure 2A Supplemental Figure 2A We resolved the 68-kDa PpiD protein in two higher molecular mass complexes with estimated molecular masses of 156 and 104 kDa (Fig. 2A and supplemental Fig. 2). Since neither of the PpiD complexes had any interacting partners in the SDS gel, we conclude that PpiD is present as both a trimer and a dimer. PpiD was present as a trimer.The 68-kDa PpiD protein was identified in two higher molecular mass complexes with estimated molecular masses of 156 and 104 kDa. ppid-ppid-1 1 18 unspecified role unspecified role neutral component neutral component physical association physical association Figure 2A Supplemental Figure 2A We resolved the 68-kDa PpiD protein in two higher molecular mass complexes with estimated molecular masses of 156 and 104 kDa (Fig. 2A and supplemental Fig. 2). Since neither of the PpiD complexes had any interacting partners in the SDS gel, we conclude that PpiD is present as both a trimer and a dimer. PpiD is present as a dimer. The 68-kDa PpiD protein in two higher molecular mass complexes with estimated molecular masses of 156 and 104 kDa. zipa-yjdb 1 2 unspecified role unspecified role neutral component neutral component 24 unspecified role unspecified role neutral component neutral component physical association physical association Figure 4A We identified ZipA in a channel with two other proteins (Fig. 4A). Although the 24-kDa interacting partner could not be identified, wE could identify YjdB (61 kDa) as an interacting partner to ZipA. A 24-kDa interacting partner could not be identified by mass spectrometry. The ZipA (36 kDa) protein was shown to interact with YjdB (61 kDa) and a 24 kDa protein which could not be identified. The molecular mass of this protein was estimated to be 91 kDa. Further studies by the author indicated this to be spurious interactions. wzzb-wzzb 1 32 unspecified role unspecified role neutral component neutral component physical association physical association Figure 2A Supplementary Figure 2 Since no interacting proteins could be detected, we concluded that WzzB is present as a dimer. WzzB is present as a dimer. The moecular mass was estimated as 70 kDa. yajc-yajc 1 31 unspecified role unspecified role neutral component neutral component 31 unspecified role unspecified role neutral component neutral component physical association physical association Figure 2A Supplemental Figure 2 YajC was present as an homoligomeric complex of molecualr mass 56 kDa. Since we could not find any interacting proteins in this complex, we conclude that YajC is present as a homo-oligomer in excess to the other components of the translocon. seca-seca 1 27 unspecified role unspecified role neutral component neutral component 27 unspecified role unspecified role neutral component neutral component physical association physical association SecA protein was shown to be a dimer with molecular mass 200 kDa. Figure 4C Using soluble molecular mass markers to estimate molecular mass, we observed that SecA resolved at 200 kDa in the BN gel (Fig. 4C), corresponding exactly to a dimer. lepb-lepb 1 8 unspecified role unspecified role neutral component neutral component 8 unspecified role unspecified role neutral component neutral component physical association physical association LepB protein (P00803) was thought to be present as a dimer with a molecular mass of 60 kDa. Figure 4D Since the LepB complex is not abundant, we could not identify interacting partners but the size of the complex in the BN gel suggests that LepB may form a dimer in the inner membrane. putp-putp 1 21 unspecified role unspecified role neutral component neutral component 21 unspecified role unspecified role neutral component neutral component physical association physical association The putP protein appeared to be a dimer with molecular mass 80 kDa. Figure 2A Supplemental Figure 2 Both the 54-kDa sodium/proline symporter (PutP) and the 59-kDa acetate permease (YjcG/ActP) are major facilitator superfamily transporters. For neither protein are we aware of any reports alluding to their existence in an oligomeric complex. However, both proteins seemed to be dimeric actp-actp 1 17 unspecified role unspecified role neutral component neutral component 17 unspecified role unspecified role neutral component neutral component physical association physical association The AtcP protein appeared to be dimeric the molecular mass was estimated as 90 kDa. Figure 2A Supplemental Figure 2 Both the 54-kDa sodium/proline symporter (PutP) and the 59-kDa acetate permease (YjcG/ActP) are major facilitator superfamily transporters. For neither protein are we aware of any reports alluding to their existence in an oligomeric complex. However, both proteins seemed to be dimeric acrb-acrb 1 14 unspecified role unspecified role neutral component neutral component physical association physical association ArcB complex was shown to be trimeric, moecular mass was estimated at 342 kDa. Figure 5 We identified AcrB (113 kDa) in a complex of 342kDa and AcrA (42 kDa) in a separate complex of 115 kDa, both corresponding to homotrimeric complexes The participant EBI-551006(P31224) was duplicated. It is posssible that originally this interaction did contain more participants pointing to different Trembl proteins which have been merged to a single swissprot protein later. acra-acra 1 28 unspecified role unspecified role neutral component neutral component physical association physical association ArcA complex was shown to be trimeric, molecular mass was estimated at 115 kDa. Figure 5 We identified AcrB (113 kDa) in a complex of 342kDa and AcrA (42 kDa) in a separate complex of 115 kDa, both corresponding to homotrimeric complexes The participant EBI-875601(P0AE06) was duplicated. It is posssible that originally this interaction did contain more participants pointing to different Trembl proteins which have been merged to a single swissprot protein later. mtde-mtde 1 29 unspecified role unspecified role neutral component neutral component physical association physical association MtdE complex was shown to be trimeric, molecualar mass was estimated at 343 kDa. Figure 5 MdtE and MdtF were identified in two separate complexes of 343 and 114 kDa, corresponding to homotrimers The participant EBI-1133856(P37636) was duplicated. It is posssible that originally this interaction did contain more participants pointing to different Trembl proteins which have been merged to a single swissprot protein later. mtdf-mtdf 1 37 unspecified role unspecified role neutral component neutral component physical association physical association MtdF complex was shown to be trimeric, molecualr mass was esimated at 114 kDa. Figure 5 MdtE and MdtF were identified in two separate complexes of 343 and 114 kDa, corresponding to homotrimers The participant EBI-906890(P37637) was duplicated. It is posssible that originally this interaction did contain more participants pointing to different Trembl proteins which have been merged to a single swissprot protein later. mscs 1 12 unspecified role unspecified role neutral component neutral component physical association physical association MscS complex was shown to be homotepameric, molecualr mass was estimated as 242 kDa. Figure 2A Supplemental Figure 2 We identified the 31-kDa MscS protein (encoded by yggB) in a complex of 242kDa (Fig. 2A and supplemental Fig. 2). No other proteins were detected in the channel, and we conclude that (MscS)7 was intact. ygu-yagu 1 38 unspecified role unspecified role neutral component neutral component 38 unspecified role unspecified role neutral component neutral component physical association physical association The YagU protein complex was shoown to be dimeric, molecualr mass was estimated as 47 kDa. Figure 2A Supplemental Figure 2. YagU has three predicted TMHs and no known biochemical function. We identified YagU (22 kDa) at 47 kDa in the BN (Fig. 2A and supplemental Fig. 2) and conclude that it is present as a dimer. ydga-ydga 1 36 unspecified role unspecified role neutral component neutral component 36 unspecified role unspecified role neutral component neutral component physical association physical association The YdgA protein complex was shoown to be dimeric, molecular mass was estimated as 116 kDa. Figure 2A Supplemental Figure 2. YdgA resolved at 106 kDa in the BN gel (Fig. 2A and supplemental Fig. 2), and we conclude that it is present as a dimer. ompf-ompf 1 15 unspecified role unspecified role neutral component neutral component physical association physical association The OmpF protein complex was trimeric, molecular mass was estimated as 37 kDa. Figure 2B We identified the 37-kDaOmpFin a predominant complex that corresponds in molecular mass to a trimer in the BN gel (relative to the soluble markers), and we conclude that (OmpF)3 is intact. The authors note that "Other OmpF forms detected in the SDS gel are a result of smearing in the BN-gel or incomplete denaturation in the SDS gel." The participant EBI-371336(P02931) was duplicated. It is posssible that originally this interaction did contain more participants pointing to different Trembl proteins which have been merged to a single swissprot protein later. lamb-lamb 1 39 unspecified role unspecified role neutral component neutral component physical association physical association The LamB protein was trimeric , molecular mass not quoted. Figure 2B We identified the 47-kDa LamB protein in a complex that corresponds in molecular mass to a trimer (again relative to soluble markers) (Fig. 2B), and we conclude that LamB3 is intact. The participant EBI-371309(P02943) was duplicated. It is posssible that originally this interaction did contain more participants pointing to different Trembl proteins which have been merged to a single swissprot protein later. tolc-tolc 1 30 unspecified role unspecified role neutral component neutral component physical association physical association TolC was trimeric, molcular mass of he complex not specified. Figure 2B We identified the 50-kDa TolC in a complex that corresponded in molecular mass to the trimer (again relative to soluble markers) (Fig. 2B), and we conclude that(TolC)3 is intact. The participant EBI-875614(P02930) was duplicated. It is posssible that originally this interaction did contain more participants pointing to different Trembl proteins which have been merged to a single swissprot protein later. nlpb-yaet-yfio 1 40 unspecified role unspecified role neutral component neutral component 13 unspecified role unspecified role neutral component neutral component 4 unspecified role unspecified role neutral component neutral component physical association physical association YaeT (85 kDa), NlpB (34 kDa), and YfiO (26 kDa), along with a fourth protein of 40 kDa, in a complex, corresponding to exactly 178 kDa was identified. Figure 2B YaeT (85 kDa), NlpB (34 kDa), and YfiO (26 kDa), along with a fourth protein of 40 kDa, in a complex, corresponding to exactly 178 kDa was identified. ompa-ompa 1 6 unspecified role unspecified role neutral component neutral component 6 unspecified role unspecified role neutral component neutral component physical association physical association OmpA was dimeric with estimated molecular mass 74 kDa. Figure 2B We identified OmpA and FadL (Fig. 2B) at the anticipated molecular masses of 30 and 33 kDa in the SDS gel; however, in contrast to the literature, both were estimated to be dimers from their molecular mass in the BN gel (OmpA at 74 kDa, FadL at 77 kDa). fadl-fadl 1 10 unspecified role unspecified role neutral component neutral component 10 unspecified role unspecified role neutral component neutral component physical association physical association FadL was dimeric with estimated molecular mass 77 kDa. Figure 2B We identified OmpA and FadL (Fig. 2B) at the anticipated molecular masses of 30 and 33 kDa in the SDS gel; however, in contrast to the literature, both were estimated to be dimers from their molecular mass in the BN gel (OmpA at 74 kDa, FadL at 77 kDa). slp-slp 1 11 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component physical association physical association Slp as appeared as a smeared band in the SDS gel indicating that it forms higher order oligomers. Figure 2B We identified Slp as a smeared band in the SDS gel (Fig. 2B), indicating that it forms higher order oligomers. muli-muli 1 16 unspecified role unspecified role neutral component neutral component 16 unspecified role unspecified role neutral component neutral component physical association physical association The 8-kDa MulI in a complex with an estimated molecular mass of 87 kDa (Fig. 2B). Other less abundant, higher molecular mass complexes were also detected. Figure 2B We detected the 8-kDa MulI in a complex with an estimated molecular mass of 87 kDa (Fig. 2B). Other less abundant, higher molecular mass complexes were also detected.