DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Conformational transition of Sec machinery inferred from bacterial SecYE structures. Conformational transition of Sec machinery inferred from bacterial SecYE structures. Nature 2008 imex curation Tsukazaki T., Mori H., Fukai S., Ishitani R., Mori T., Dohmae N., Perederina A., Sugita Y., Vassylyev DG., Ito K., Nureki O. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Tsukazaki T., Mori H., Fukai S., Ishitani R., Mori T., Dohmae N., Perederina A., Sugita Y., Vassylyev DG., Ito K., Nureki O. DIP original experiment: DIP-250213X Nature 2008 IMEx Conformational transition of Sec machinery inferred from bacterial SecYE structures. Conformational transition of Sec machinery inferred from bacterial SecYE structures. Conformational transition of Sec machinery inferred from bacterial SecYE structures. Nature 2008 imex curation Tsukazaki T., Mori H., Fukai S., Ishitani R., Mori T., Dohmae N., Perederina A., Sugita Y., Vassylyev DG., Ito K., Nureki O. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Tsukazaki T., Mori H., Fukai S., Ishitani R., Mori T., Dohmae N., Perederina A., Sugita Y., Vassylyev DG., Ito K., Nureki O. DIP original experiment: DIP-250214X Nature 2008 IMEx Conformational transition of Sec machinery inferred from bacterial SecYE structures. Conformational transition of Sec machinery inferred from bacterial SecYE structures. Conformational transition of Sec machinery inferred from bacterial SecYE structures. Nature 2008 imex curation Tsukazaki T., Mori H., Fukai S., Ishitani R., Mori T., Dohmae N., Perederina A., Sugita Y., Vassylyev DG., Ito K., Nureki O. 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 Tsukazaki T., Mori H., Fukai S., Ishitani R., Mori T., Dohmae N., Perederina A., Sugita Y., Vassylyev DG., Ito K., Nureki O. DIP original experiment: DIP-250212X Nature 2008 IMEx Conformational transition of Sec machinery inferred from bacterial SecYE structures. seca_thet8 Protein translocase subunit SecA secA TTHA1251 protein protein thet8 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) MLGLLRRLFDNNEREIARYYKQVVEPVNRLEAEVEKLPDLAAAYRELKEKHEKGASLDELLPMAFALTRESAKRYLGMRHFDVQLIGGAVLHEGKIAEMKTGEGKTLVATLAVALNALTGKGVHVVTVNDYLARRDAEWMGPVYRGLGLSVGVIQHASTPAERRKAYLADVTYVTNSELGFDYLRDNMAISPDQLVLRHDHPLHYAIIDEVDSILIDEARTPLIISGPAEKATDLYYKMAEIAKKLERGLPAEPGVRKEPTGDYTVEEKNRSVHLTLQGIAKAEKLLGIEGLFSPENMELAHMLIQAIRAKELYHRDRDYIVQDGQVIIVDEFTGRLMPGRRYGEGLHQAIEAKEGVRIERENQTLATITYQNFFRLYEKRAGMTGTAKTEEKEFQEIYGMDVVVVPTNRPVIRKDFPDVVYRTEKGKFYAVVEEIAEKYERGQPVLVGTISIEKSERLSQMLKEPRLYLPRLEMRLELFKKASQKQQGPEWERLRKLLERPAQLKDEDLAPFEGLIPPKGNLRTAWEGLKRAVHTLAVLRQGIPHQVLNAKHHAREAEIVAQAGRSKTVTIATNMAGRGTDIKLGGNPEYLAAALLEKEGFDRYEWKVELFIKKMVAGKEEEARALAQELGIREELLERIREIREECKQDEERVRALGGLFIIGTERHESRRIDNQLRGRAGRQGDPGGSRFYVSFDDDLMRLFASDRVIAMLDRMGFDDSEPIEHPMVTRSIERAQKRVEDRNFAIRKQLLQFDDVLSRQREVIYAQRRLILLGKDEEVKEAAIGMVEETVASLAENFLNPEVHPEDWDLEGLKATLLDTAPQLQDFPFAELRALKAEEAVERLVEAALKAYEAREAELSPPLMRAVERFVILNVVDNAWKEHLHNLDVLRQGIFLRGYGQKDPFQEYKIEATRLFNEMVAFIKSEVAKFLFRLKVEAEPVRPVREAPYVPVPEAKPEPSEVFGVERKRATPPPQPGLSRAERRRLMRQEKKRKK 9A22888B52698CCA q8kzp4_theth Protein translocase subunit SecE TthHB5018_01280 secE TTMY_1743 TTHN1_01760 TthAA229_01400 protein protein theth Thermus thermophilus MFARLIRYFQEARAELARVTWPTREQVVEGTQAILLFTLAFMVILGLYDTVFRFLIGLLR DIP protein Q8KZP4 original sequence version: 32 q8kzp3_theth Protein translocase subunit SecY secY TTHN1_02242 protein protein theth Thermus thermophilus MLKAFWSALQIPELRQRVLFTLLVLAAYRLGAFIPTPGVDLDKIQEFLRTAQGGVFGIINLFSGGNFERFSIFALGIMPYITAAIIMQILVTVVPALEKLSKEGEEGRRIINQYTRIGGIALGAFQGFFLATAFLGAEGGRFLLPGWSPGPFFWFVVVVTQVAGIALLLWMAERITEYGIGNGTSLIIFAGIVVEWLPQILRTIGLIRTGEVNLVAFLFFLAFIVLAFAGMAAVQQAERRIPVQYARKVVGRRVYGGQATYIPIKLNAAGVIPIIFAAAILQIPIFLAAPFQDNPVLQGIANFFNPTRPSGLFIEVLLVILFTYVYTAVQFDPKRIAESLREYGGFIPGIRPGEPTVKFLEHIVSRLTLWGALFLGLVTLLPQIIQNLTGIHSIAFSGIGLLIVVGVALDTLRQVESQLMLRSYEGFLSRGRLRGRNR DIP protein Q8KZP3 original sequence version: 39 sece-secy-1 3 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction sece-secy-2 1 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction seca-secy-5 2 4 unspecified role unspecified role unspecified role unspecified role Q5SIW3:p.Pro202Cys P202C mutation mutation certain certain sequence position certain certain certain sequence position certain P C This feature has been corrected as a result of our quality control procedures. The original label was 'P202C'. Wed May 02 17:24:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro202cys' Tue Jun 30 17:00:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro202Cys' Q5SIW3:p.Leu775Cys L775C mutation mutation certain certain sequence position certain certain certain sequence position certain L C This feature has been corrected as a result of our quality control procedures. The original label was 'L775C'. Wed May 02 20:11:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu775cys' Tue Jun 30 16:28:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu775Cys' ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role Q8KZP3:p.Ala259Cys A259C mutation mutation certain certain sequence position certain certain certain sequence position certain A C This feature has been corrected as a result of our quality control procedures. The original label was 'A259C'. Wed May 02 15:14:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala259cys' Tue Jun 30 19:49:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala259Cys' Q8KZP3:p.Pro352Cys P352C mutation mutation certain certain sequence position certain certain certain sequence position certain P C This feature has been corrected as a result of our quality control procedures. The original label was 'P352C'. Wed May 02 18:27:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro352cys' Tue Jun 30 19:18:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro352Cys' ecolx Escherichia coli direct interaction direct interaction