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/ Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ. Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ. J. Biol. Chem. (0021-9258) 1999 imex curation Suh WC., Lu CZ., Gross CA. cgross@cgl.ucsf.edu 09-April-2009: Contacted by JYOTI. orchard Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Suh WC., Lu CZ., Gross CA. cgross@cgl.ucsf.edu Accepted 2009-APR-12 by ORCHARD. 09-April-2009: Contacted by JYOTI. J. Biol. Chem. (0021-9258) 1999 orchard Only protein-protein interactions imex curation dnak_ecoli Chaperone protein DnaK dnaK groP grpF seg b0014 Heat shock protein 70 Heat shock 70 kDa protein HSP70 JW0013 protein protein ecoli Escherichia coli (strain K12) MGKIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQRDVSIMPFKIIAADNGDAWVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKGTGNRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVLATNGDTHLGGEDFDSRLINYLVEEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVALQDAGLSVSDIDDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGDVKDVLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHAQQQTAGADASANNAKDDDVVDAEFEEVKDKK DIP protein P0A6Y8 original sequence version: 44 DIP protein P0A6Y8 original sequence version: 96 DIP protein P0A6Y8 original sequence version: 91 DIP protein P0A6Y8 original sequence version: 119 DIP protein P0A6Y8 original sequence version: 95 5A8589B21D7CD9C1 dnaj_ecoli Chaperone protein DnaJ dnaJ groP b0015 Heat shock protein J HSP40 JW0014 protein protein ecoli Escherichia coli (strain K12) MAKQDYYEILGVSKTAEEREIRKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNERQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR DIP protein P08622 original sequence version: 105 DIP protein P08622 original sequence version: 118 DIP protein P08622 original sequence version: 152 DIP protein P08622 original sequence version: null 05FA762EF9844532 dnaj-dnak 1 2 unspecified role unspecified role prey prey P0A6Y8:p.Asp201Asn mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain D N Wed May 02 19:11:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp201asn' Tue Jun 30 20:06:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp201Asn' P0A6Y8:p.Thr199Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain T A Wed May 02 16:37:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr199ala' Tue Jun 30 19:40:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr199Ala' n terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 3 unspecified role unspecified role bait bait c terminal biotin tag biotin tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range physical association physical association 1, 2, 3 Only the ATP bound form of DnaK bound the DnaJ The apparent ka and kd values were 1.47 x 104 M-1 s-1 and 8.0 x 10-3 s-1, respectively. The binding affinity of DnaJ108-Bccp to DnaK in the presence of ATP is comparable to that of full-length DnaJ,whereas DnaJ76-Bccp binds with somewhat lower affinity. Temp = 25C, pH=7.6 dnaj-dnak-1 1 3 unspecified role unspecified role bait bait c terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range n terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 2 unspecified role unspecified role prey prey physical association physical association 4A the J-domain alone neither stimulates ATP hydrolysis nor binds to DnaK in the reaction detected in the Biacore. DnaK bound to ATP used for the experiment. dnaj-dnak-2 1 2 unspecified role unspecified role prey prey 3 unspecified role unspecified role bait bait P08622:p.Lys62Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain K A Wed May 02 15:19:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys62ala' Tue Jun 30 17:19:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys62Ala' P08622:p.Arg63Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain R A Wed May 02 15:02:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg63ala' Tue Jun 30 18:06:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg63Ala' P08622:p.[Lys62Ala;Arg63Ala] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain R A Wed May 02 16:45:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys62ala,arg63ala' Tue Jun 30 15:43:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys62Ala;Arg63Ala]' c terminal bccp biotin tag biotin tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range n terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association 4A, 4B DnaK bound to ATP used for the experiment. The binding affinity of DnaJ108-Bccp to DnaK in the presence of ATP is comparable to that of full-length DnaJ, whereas DnaJ76-Bccp binds with somewhat lower affinity (Fig. 4A).