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/ Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 imex curation Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - niko@brandeis.edu,deaconescua@janelia.hhmi.org 18-Feb-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - niko@brandeis.edu,deaconescua@janelia.hhmi.org Accepted 2014-JAN-20 by MGT Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 Only protein-protein interactions imex curation Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 imex curation Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - niko@brandeis.edu,deaconescua@janelia.hhmi.org 18-Feb-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - niko@brandeis.edu,deaconescua@janelia.hhmi.org Accepted 2014-JAN-20 by MGT Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 Only protein-protein interactions imex curation Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 imex curation Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - niko@brandeis.edu,deaconescua@janelia.hhmi.org 18-Feb-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink tag visualisation tag visualisation Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - Crosslinking was achieved by increasing exposure to UV radiation. Protein was visualised by Coomassie staining and the bound ATP by phosphor imaging. niko@brandeis.edu,deaconescua@janelia.hhmi.org Accepted 2014-JAN-20 by MGT Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 Only protein-protein interactions imex curation Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 imex curation Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - niko@brandeis.edu,deaconescua@janelia.hhmi.org 18-Feb-2014: 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 Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - niko@brandeis.edu,deaconescua@janelia.hhmi.org Accepted 2014-JAN-20 by MGT Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 Only protein-protein interactions imex curation Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 imex curation Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - niko@brandeis.edu,deaconescua@janelia.hhmi.org 18-Feb-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro atpase assay atpase assay predetermined predetermined participant predetermined Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Mfd constructs were first reduced with tris(2-carboxyethyl)phosphine. For assays using the oxidised state constructs were oxidised with phenanthroline resulting in the formation of disulfide bonds between the residues mutated to cysteine. The oxidised states of all variants of Mfd had reduced ATPase activity compared to their respective reduced states. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - niko@brandeis.edu,deaconescua@janelia.hhmi.org Accepted 2014-JAN-20 by MGT Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 Only protein-protein interactions imex curation Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 imex curation Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - niko@brandeis.edu,deaconescua@janelia.hhmi.org 18-Feb-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro protease assay protease assay weight by comassie molecular weight estimation by coomasie staining weight by comassie Deaconescu A.M., Sevostyanova A., Artsimovitch I., Grigorieff N. Complexes were not further purified before they were separated by SDS-PAGE (I wrote to the author). They were only looking at the changes in the disulfide bonding. Therefore I cannot capture the potential interaction of Mfd with UvrA for those expts (where UvrA was visible on the gel in teh first place) (Fig 4d, S3c & S7b). - Fig. 4e: 'TEC' consists of open transcription fork and newly-synthesised RNA so expt is only DNA bdg. - Fig. S2f: probably just DNA bdg again as there is no evidence that RNAP actually interacts with TRCF, they just bind to adjacent region of DNA! The DNA template is a synthetic bit of DNA including the transcription promoter region. - Fig. S3a: 'Trysin' is bovine (confirmed by author) but there are two entries in Uniprot (P00760 & Q29463) and the Sigma page doesn't have further info as to which one it might be so interaction has not been captured. - niko@brandeis.edu,deaconescua@janelia.hhmi.org Accepted 2014-JAN-20 by MGT Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 2012 Only protein-protein interactions imex curation mfd_ecoli Transcription-repair-coupling factor mfd b1114 JW1100 protein protein ecoli Escherichia coli (strain K12) MPEQYRYTLPVKAGEQRLLGELTGAACATLVAEIAERHAGPVVLIAPDMQNALRLHDEISQFTDQMVMNLADWETLPYDSFSPHQDIISSRLSTLYQLPTMQRGVLIVPVNTLMQRVCPHSFLHGHALVMKKGQRLSRDALRTQLDSAGYRHVDQVMEHGEYATRGALLDLFPMGSELPYRLDFFDDEIDSLRVFDVDSQRTLEEVEAINLLPAHEFPTDKAAIELFRSQWRDTFEVKRDPEHIYQQVSKGTLPAGIEYWQPLFFSEPLPPLFSYFPANTLLVNTGDLETSAERFQADTLARFENRGVDPMRPLLPPQSLWLRVDELFSELKNWPRVQLKTEHLPTKAANANLGFQKLPDLAVQAQQKAPLDALRKFLETFDGPVVFSVESEGRREALGELLARIKIAPQRIMRLDEASDRGRYLMIGAAEHGFVDTVRNLALICESDLLGERVARRRQDSRRTINPDTLIRNLAELHIGQPVVHLEHGVGRYAGMTTLEAGGITGEYLMLTYANDAKLYVPVSSLHLISRYAGGAEENAPLHKLGGDAWSRARQKAAEKVRDVAAELLDIYAQRAAKEGFAFKHDREQYQLFCDSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVDNHKQVAVLVPTTLLAQQHYDNFRDRFANWPVRIEMISRFRSAKEQTQILAEVAEGKIDILIGTHKLLQSDVKFKDLGLLIVDEEHRFGVRHKERIKAMRANVDILTLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTFVREYDSMVVREAILREILRGGQVYYLYNDVENIQKAAERLAELVPEARIAIGHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRGRVGRSHHQAYAWLLTPHPKAMTTDAQKRLEAIASLEDLGAGFALATHDLEIRGAGELLGEEQSGSMETIGFSLYMELLENAVDALKAGREPSLEDLTSQQTEVELRMPSLLPDDFIPDVNTRLSFYKRIASAKTENELEEIKVELIDRFGLLPDPARTLLDIARLRQQAQKLGIRKLEGNEKGGVIEFAEKNHVNPAWLIGLLQKQPQHYRLDGPTRLKFIQDLSERKTRIEWVRQFMRELEENAIA DIP protein P30958 original sequence version: null 8E0D149306C8C31C subc_bacli Subtilisin Carlsberg subC apr protein protein bacli Bacillus licheniformis MMRKKSFWLGMLTAFMLVFTMAFSDSASAAQPAKNVEKDYIVGFKSGVKTASVKKDIIKESGGKVDKQFRIINAAKAKLDKEALKEVKNDPDVAYVEEDHVAHALAQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYAKGVVVVAAAGNSGSSGNTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides mint 38432C04FFA048C1 atp ATP Adenosine 5'-triphosphate Adenosine triphosphate ADENOSINE-5'-TRIPHOSPHATE Adephos Adetol Adynol Atipi ATP Atriphos Cardenosine Fosfobion Glucobasin H4atp Myotriphos Triadenyl Triphosphaden adenosine 5'-(tetrahydrogen triphosphate) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) adp adenosine 5'-(trihydrogen diphosphate) (ADP) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) uvra_ecoli UvrABC system protein A uvrA dinE b4058 Excinuclease ABC subunit A JW4019 protein protein ecoli Escherichia coli (strain K12) MDKIEVRGARTHNLKNINLVIPRDKLIVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPAISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPDHDVPLAAQTVSQMVDNVLSQPEGKRLMLLAPIIKERKGEHTKTLENLASQGYIRARIDGEVCDLSDPPKLELQKKHTIEVVVDRFKVRDDLTQRLAESFETALELSGGTAVVADMDDPKAEELLFSANFACPICGYSMRELEPRLFSFNNPAGACPTCDGLGVQQYFDPDRVIQNPELSLAGGAIRGWDRRNFYYFQMLKSLADHYKFDVEAPWGSLSANVHKVVLYGSGKENIEFKYMNDRGDTSIRRHPFEGVLHNMERRYKETESSAVREELAKFISNRPCASCEGTRLRREARHVYVENTPLPAISDMSIGHAMEFFNNLKLAGQRAKIAEKILKEIGDRLKFLVNVGLNYLTLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLIHLRDLGNTVIVVEHDEDAIRAADHVIDIGPGAGVHGGEVVAEGPLEAIMAVPESLTGQYMSGKRKIEVPKKRVPANPEKVLKLTGARGNNLKDVTLTLPVGLFTCITGVSGSGKSTLINDTLFPIAQRQLNGATIAEPAPYRDIQGLEHFDKVIDIDQSPIGRTPRSNPATYTGVFTPVRELFAGVPESRARGYTPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDIYVPCDQCKGKRYNRETLEIKYKGKTIHEVLDMTIEEAREFFDAVPALARKLQTLMDVGLTYIRLGQSATTLSGGEAQRVKLARELSKRGTGQTLYILDEPTTGLHFADIQQLLDVLHKLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGEILVSGTPETVAECEASHTARFLKPML DIP protein P0A698 original sequence version: 81 DIP protein P0A698 original sequence version: 82 DIP protein P0A698 original sequence version: 41 DIP protein P0A698 original sequence version: null D61AAEB6514B860C a5pjb8_bovin CTRB1 LOC618826 protein protein bovin Bos taurus (Bovine) Bovine MALLWVVLGFFLFGSSFGCGVPAIDPVLSGLSRIVNGEDAVPGSWPWQVSLQTSSGFHFCGGSLISEDWVVTAAHCGVRKGHLVVAGVSDQGSEEEAGQVLRVAEVFEHPQWDLRAVRNDVALLKLAAPARLSAAVAPVCLPSADTSFPTGSLCTVTGWGKTRYNAFDTPDKLQQATLPILSNADCREFWGSKITDVMICAGASGISSCMGDSGGPLVCQKDGAWTLAGIVSWGSSRCSPFLPGVYARVTKFIPWILEVLEAN 717F94F9148C4990 mfd-uvra 4 7 unspecified role unspecified role neutral component neutral component 127-213 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 11 unspecified role unspecified role neutral component neutral component 131-250 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 17 15 direct interaction direct interaction Table S1 Rwork = 0.24, Rfree = 0.28 2.8 A mfd-uvra-2 1 11 unspecified role unspecified role prey prey 131-250 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role bait bait 127-213 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 ecoli Escherichia coli (strain K12) 20 22 direct interaction direct interaction Fig. S1a atp-mfd 2 9 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 7 unspecified role unspecified role neutral component neutral component 479-1148 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P30958:p.Glu730Gln mutation mutation certain certain sequence position certain certain certain sequence position certain E Q Wed May 02 19:20:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu730gln' Tue Jun 30 15:56:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu730Gln' 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 ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig 3b, S6a, S6b adp-mfd 2 10 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 7 unspecified role unspecified role neutral component neutral component P30958:p.Glu730Gln mutation mutation certain certain sequence position certain certain certain sequence position certain E Q Wed May 02 15:33:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu730gln' Tue Jun 30 18:59:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu730Gln' 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 479-1148 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 Fig 3b, S6a atp-mfd-2 5 7 enzyme enzyme neutral component neutral component P30958:p.[His527Cys;Ala1031Cys] mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain H C certain certain sequence position certain certain certain sequence position certain A C Wed May 02 14:29:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his527cys,ala1031cys' Tue Jun 30 18:23:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[His527Cys;Ala1031Cys]' P30958:p.[Ala167Cys;Gly1051Cys] mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain G C certain certain sequence position certain certain certain sequence position certain A C Fri Jul 22 11:02:27 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'gly1051cys,ala167cys' Wed May 02 16:56:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala167cys,gly1051cys' Tue Jun 30 18:08:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ala167Cys;Gly1051Cys]' P30958:p.Glu730Gln mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain E Q Wed May 02 17:33:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu730gln' Tue Jun 30 16:00:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu730Gln' 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 ecoli Escherichia coli (strain K12) 9 enzyme target enzyme target substrate substrate neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) atpase reaction atpase reaction Fig. 4a atp-mfd-5 3 9 competitor competitor competitor neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 9 unspecified role unspecified role neutral component neutral component region 32p radiolabel 32p radiolabel P32 32P 32P P32 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined chemical synthesis Chemical synthesis (Chemical synthesis) 7 unspecified role unspecified role 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 ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. S2a mfd-subtilisin 6 8 enzyme enzyme neutral component neutral component bacli Bacillus licheniformis 7 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 ecoli Escherichia coli (strain K12) protein cleavage protein cleavage Fig. S3a mfd-chymotrypsin-1 6 7 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 ecoli Escherichia coli (strain K12) 12 enzyme enzyme neutral component neutral component bovin Bos taurus (Bovine) Bovine protein cleavage protein cleavage Fig. S3a mfd-atp 3 7 unspecified role unspecified role 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 ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role neutral component neutral component region 32p radiolabel 32p radiolabel P32 32P 32P P32 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction Fig. S2a