DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. 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 Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254863X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254869X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254866X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. 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 Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254865X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254867X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254871X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254870X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254872X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254864X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254861X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254868X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. 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 Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254860X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Imada K., Minamino T., Kinoshita M., Furukawa Y., Namba K. DIP original experiment: DIP-254862X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. flij_salty Flagellar FliJ protein flaO flaS STM1973 fliJ protein protein salty Salmonella typhimurium MAQHGALETLKDLAEKEVDDAARLLGEMRRGCQQAEEQLKMLIDYQNEYRSNLNTDMGNGIASNRWINYQQFIQTLEKAIEQHRLQLTQWTQKVDLALKSWREKKQRLQAWQTLQDRQTAAALLAENRMDQKKMDEFAQRAAMRKPE DIP protein P0A1K1 original sequence version: 70 34451B5F4514AF08 flic_salty Flagellin fliC flaF hag Phase 1-I flagellin STM1959 protein protein salty Salmonella typhimurium MAQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAQTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDTLNVQQKYKVSDTAATVTGYADTTIALDNSTFKASATGLGGTDQKIDGDLKFDDTTGKYYAKVTVTGGTGKDGYYEVSVDKTNGEVTLAGGATSPLTGGLPATATEDVKNVQVANADLTEAKAALTAAGVTGTASVVKMSYTDNNGKTIDGGLAVKVGDDYYSATQNKDGSISINTTKYTADDGTSKTALNKLGGADGKTEVVSIGGKTYAASKAEGHNFKAQPDLAEAAATTTENPLQKIDAALAQVDTLRSDLGAVQNRFNSAITNLGNTVNNLTSARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR 4BD7849FA3B936BA 4BD7849FA3B936BA flii_salty Flagellum-specific ATP synthase fliI fla AIII flaC STM1972 protein protein salty Salmonella typhimurium MTTRLTRWLTALDNFEAKMALLPAVRRYGRLTRATGLVLEATGLQLPLGATCIIERQDGPETKEVESEVVGFNGQRLFLMPLEEVEGILPGARVYARNGHGDGLQSGKQLPLGPALLGRVLDGGGKPLDGLPAPDTLETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGPDGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIHGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALITEQHYARVRLFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAITLWPQLEAFLQQGIFERADWEDSLQALDLIFPTV 830867B657592BF1 830867B657592BF1 flit_salty Flagellar protein FliT fliT STM1962 protein protein salty Salmonella typhimurium MTSTVEFINRWQRIALLSQSLLELAQRGEWDLLLQQEVSYLQSIETVMEKQTPPGITRSIQDMVAGYIKQTLDNEQLLKGLLQQRLDELSSLIGQSTRQKSLNNAYGRLSGMLLVPDAPGAS DIP protein P0A1N2 original sequence version: 64 flid_salty Flagellar hook-associated protein 2 fliD Filament cap protein Flagellar cap protein flaV flbC STM1960 protein protein salty Salmonella typhimurium MASISSLGVGSNLPLDQLLTDLTKNEKGRLTPITKQQSANSAKLTAYGTLKSALEKFQTANTALNKADLFKSTVASSTTEDLKVSTTAGAAAGTYKINVTQLAAAQSLATKTTFATTKEQLGDTSVTSRTIKIEQPGRKEPLEIKLDKGDTSMEAIRDAINDADSGIAASIVKVKENEFQLVLTANSGTDNTMKITVEGDTKLNDLLAYDSTTNTGNMQELVKAENAKLNVNGIDIERQSNTVTDAPQGITLTLTKKVTDATVTVTKDDTKAKEAIKSWVDAYNSLVDTFSSLTKYTAVEPGEEASDKNGALLGDSVVRTIQTGIRAQFANSGSNSAFKTMAEIGITQDGTSGKLKIDDDKLTKVLKDNTAAARELLVGDGKETGITTKIATEVKSYLADDGIIDNAQDNVNATLKSLTKQYLSVSNSIDETVARYKAQFTQLDTMMSKLNNTSSYLTQQFTAMNKS 5C1BD69A1F233BEA flit-1 12 17 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction flit-2 10 17 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction flit-flii-2 5 16 unspecified role unspecified role prey prey His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 17 unspecified role unspecified role bait bait Region 2-94 Region 2-94 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association flit-flii-3 7 16 unspecified role unspecified role prey prey His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 17 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 2-94 Region 2-94 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction flit-flij-2 6 17 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 2-94 Region 2-94 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 unspecified role unspecified role prey prey His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction flit-3 13 17 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction flid-flit-4 1 18 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction flit-flic-1 8 15 unspecified role unspecified role prey prey ecolx Escherichia coli 17 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 2-94 Region 2-94 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association flid-flit-5 9 18 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction flit-flij-3 11 17 unspecified role unspecified role bait bait Region 2-94 Region 2-94 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 14 unspecified role unspecified role prey prey His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association flid-1 4 18 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction flit-flic-2 2 15 unspecified role unspecified role prey prey ecolx Escherichia coli 18 unspecified role unspecified role prey prey ecolx Escherichia coli 17 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 2-94 Region 2-94 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli association association flit-flid-2 3 18 unspecified role unspecified role prey prey ecolx Escherichia coli 17 unspecified role unspecified role bait bait Region 2-94 Region 2-94 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P0A1N2:p.Lys79Ala K79A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain K A This feature has been corrected as a result of our quality control procedures. The original label was 'K79A'. Wed May 02 16:41:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys79ala' Tue Jun 30 20:16:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys79Ala' P0A1N2:p.Glu75Ala E75A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain E A This feature has been corrected as a result of our quality control procedures. The original label was 'E75A'. Wed May 02 14:51:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu75ala' Tue Jun 30 18:39:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu75Ala' GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association