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 periplasmic component of a tripartite macrolide-specific efflux pump. Crystal structure of the periplasmic component of a tripartite macrolide-specific efflux pump. J. Mol. Biol. (0022-2836) 2009 imex curation Yum S., Xu Y., Piao S., Sim S.H., Kim H.M., Jo W.S., Kim K.J., Kweon H.S., Jeong M.H., Jeon H., Lee K., Ha N.C. The Aa MacA crystal (electron density maps in Fig.s S1 & S2) has not been curated as it was originally published in another paper (pmid: 18453709) and no structures have been submitted to PDB. hnc@pusan.ac.kr 22-Nov-2013: Contacted by IntAct-Help. 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 Yum S., Xu Y., Piao S., Sim S.H., Kim H.M., Jo W.S., Kim K.J., Kweon H.S., Jeong M.H., Jeon H., Lee K., Ha N.C. The Aa MacA crystal (electron density maps in Fig.s S1 & S2) has not been curated as it was originally published in another paper (pmid: 18453709) and no structures have been submitted to PDB. hnc@pusan.ac.kr Accepted 2013-NOV-11 by PPORRAS 22-Nov-2013: Contacted by IntAct-Help. J. Mol. Biol. (0022-2836) 2009 Only protein-protein interactions imex curation Crystal structure of the periplasmic component of a tripartite macrolide-specific efflux pump. Crystal structure of the periplasmic component of a tripartite macrolide-specific efflux pump. J. Mol. Biol. (0022-2836) 2009 imex curation Yum S., Xu Y., Piao S., Sim S.H., Kim H.M., Jo W.S., Kim K.J., Kweon H.S., Jeong M.H., Jeon H., Lee K., Ha N.C. The Aa MacA crystal (electron density maps in Fig.s S1 & S2) has not been curated as it was originally published in another paper (pmid: 18453709) and no structures have been submitted to PDB. hnc@pusan.ac.kr 22-Nov-2013: 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 Yum S., Xu Y., Piao S., Sim S.H., Kim H.M., Jo W.S., Kim K.J., Kweon H.S., Jeong M.H., Jeon H., Lee K., Ha N.C. The Aa MacA crystal (electron density maps in Fig.s S1 & S2) has not been curated as it was originally published in another paper (pmid: 18453709) and no structures have been submitted to PDB. hnc@pusan.ac.kr Accepted 2013-NOV-11 by PPORRAS 22-Nov-2013: Contacted by IntAct-Help. J. Mol. Biol. (0022-2836) 2009 Only protein-protein interactions imex curation Crystal structure of the periplasmic component of a tripartite macrolide-specific efflux pump. Crystal structure of the periplasmic component of a tripartite macrolide-specific efflux pump. J. Mol. Biol. (0022-2836) 2009 imex curation Yum S., Xu Y., Piao S., Sim S.H., Kim H.M., Jo W.S., Kim K.J., Kweon H.S., Jeong M.H., Jeon H., Lee K., Ha N.C. The Aa MacA crystal (electron density maps in Fig.s S1 & S2) has not been curated as it was originally published in another paper (pmid: 18453709) and no structures have been submitted to PDB. hnc@pusan.ac.kr 22-Nov-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Yum S., Xu Y., Piao S., Sim S.H., Kim H.M., Jo W.S., Kim K.J., Kweon H.S., Jeong M.H., Jeon H., Lee K., Ha N.C. The Aa MacA crystal (electron density maps in Fig.s S1 & S2) has not been curated as it was originally published in another paper (pmid: 18453709) and no structures have been submitted to PDB. hnc@pusan.ac.kr Accepted 2013-NOV-11 by PPORRAS 22-Nov-2013: Contacted by IntAct-Help. J. Mol. Biol. (0022-2836) 2009 Only protein-protein interactions imex curation maca_ecoli Macrolide export protein MacA macA b0878 ybjY JW0862 protein protein ecoli Escherichia coli (strain K12) MKKRKTVKKRYVIALVIVIAGLITLWRILNAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTYSRQQRLAQTKAVSQQDLDTAATEMAVKQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSAMLVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGQIKDVLPTPEKVNDAIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALGDPVGDNRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVVIGEAKPGAAQ DIP protein P75830 original sequence version: 82 DIP protein P75830 original sequence version: 88 DIP protein P75830 original sequence version: null 8BF287DA03B92AF9 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 q2ehl9_aggac macA protein protein aggac Aggregatibacter actinomycetemcomitans MKKKPLIITAIAAAVITGGYFFVRDSSAQTTYLTEEVKRGNIEKNVVATGSIESINTVDVGAQVSGKVTKLYVKLGQQVKKGDLIAEIDSTTQINTLNTRKAALASYQAQLVARKTAYDVALSNYNRLSKLYGQKATSLDTLNTAKATLNNAKAEMDVVQENIKQAEIEVNTAETNVGYTKITSPIDGTVISTPVSEGQTVNSNQTTPTIIKVADLSKMRIKPEISEGDITKVKAGQDVTFTILSDNKTVYHAKIDSVDPATTTISDNSSSNSSSSGSSSSSGSSSSAVYYYANIIVENPEHVLRIGMTTENNIKIADVQNVLFIPNLAVQKQQDKYVVNVLNGNTTQEREIEIGVQNDFQTEVKSGLTEGEKVVISQVAAGETFGDPDAPIIF 35F0213787A16884 maca-xray-ec 2 4 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 Fig.s 1b, 1c, 1d, 2, 3, S4 All = 0.29; Rwork = 0.28; Rfree = 0.35 2.99 A maca-molsiev-aa 1 6 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 Fig. 4a, S6 Two truncated WT versions of this protein were put through the filter column: 20-394 aa and 38-318 aa. The estimated molecular weight of the filtered products (210 and 200 kD) corresponds roughly to a hexameric conformation. The shorter construct (38-318 aa) also elutes at 60 kD which corresponds roughly to a dimer (Fig. S6). The authors state in the legend: "Aa MacA is hexameric in solution." The crystal structure (Fig.s 1-3) and electron microscopy picture (Fig. 4b) also suggests a hexameric conformation. maca-em-aa 3 6 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 Fig. 4b, S5, S7 maca-molsiev-ec 1 4 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 Fig. 4a acra-molsiev-ec 1 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 4a The authors do not give the length of this construct while the other proteins were all expressed as slightly truncated versions. maca-molsiev-aa-hexamer 1 6 unspecified role unspecified role neutral component neutral component Q2EHL9:p.Glu227Ala mutation mutation certain certain sequence position certain certain certain sequence position certain E A Wed May 02 15:24:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu227ala' Tue Jun 30 16:34:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu227Ala' 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 Fig. 5b (upper panel) The estimated molecular weight of the WT of the filtered product corresponds roughly to a hexameric conformation (210 kD). 2/3 of this mutant elute in roughly hexamers while the remaining 1/3 elutes as roughly dimers (70 kD). maca-molsiev-aa-hexamer-2 1 6 unspecified role unspecified role neutral component neutral component Q2EHL9:p.[Glu227Ala;Tyr291Ala] mutation mutation certain certain sequence position certain certain certain sequence position certain E A certain certain sequence position certain certain certain sequence position certain Y A Wed May 02 20:06:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu227ala,tyr291ala' Tue Jun 30 18:51:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu227Ala;Tyr291Ala]' 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 Fig. 5b (lower panel) The estimated molecular weight of the WT of the filtered product corresponds roughly to a hexameric conformation (210 kD). This double mutant elutes at roughly the size of a trimer (120 kD) and dimer (70 kD). maca-molsiev-aa-dimer 1 6 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 Q2EHL9:p.Glu227Ala mutation mutation certain certain sequence position certain certain certain sequence position certain E A Wed May 02 15:01:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu227ala' Tue Jun 30 20:04:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu227Ala' ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 5b (upper panel) The estimated molecular weight of the WT of the filtered product corresponds roughly to a hexameric conformation (210 kD). 2/3 of this mutant elute in roughly hexamers while the remaining 1/3 elutes as roughly dimers (70 kD). maca-molsiev-aa-trimer-2 1 6 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 Q2EHL9:p.[Glu227Ala;Tyr291Ala] mutation mutation certain certain sequence position certain certain certain sequence position certain E A certain certain sequence position certain certain certain sequence position certain Y A Wed May 02 15:30:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu227ala,tyr291ala' Tue Jun 30 16:15:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu227Ala;Tyr291Ala]' ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 5b (lower panel) The estimated molecular weight of the WT of the filtered product corresponds roughly to a hexameric conformation (210 kD). This double mutant elutes at roughly the size of a trimer (120 kD) and dimer (70 kD). maca-molsiev-aa-dimer-2 1 6 unspecified role unspecified role neutral component neutral component Q2EHL9:p.[Glu227Ala;Tyr291Ala] mutation mutation certain certain sequence position certain certain certain sequence position certain E A certain certain sequence position certain certain certain sequence position certain Y A Wed May 02 15:07:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu227ala,tyr291ala' Tue Jun 30 19:31:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu227Ala;Tyr291Ala]' 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 Fig. 5b (lower panel) The estimated molecular weight of the WT of the filtered product corresponds roughly to a hexameric conformation (210 kD). This double mutant elutes at roughly the size of a trimer (120 kD) and dimer (70 kD).