#ID(s) interactor A ID(s) interactor B Alt. ID(s) interactor A Alt. ID(s) interactor B Alias(es) interactor A Alias(es) interactor B Interaction detection method(s) Publication 1st author(s) Publication Identifier(s) Taxid interactor A Taxid interactor B Interaction type(s) Source database(s) Interaction identifier(s) Confidence value(s) Expansion method(s) Biological role(s) interactor A Biological role(s) interactor B Experimental role(s) interactor A Experimental role(s) interactor B Type(s) interactor A Type(s) interactor B Xref(s) interactor A Xref(s) interactor B Interaction Xref(s) Annotation(s) interactor A Annotation(s) interactor B Interaction annotation(s) Host organism(s) Interaction parameter(s) Creation date Update date Checksum(s) interactor A Checksum(s) interactor B Interaction Checksum(s) Negative Feature(s) interactor A Feature(s) interactor B Stoichiometry(s) interactor A Stoichiometry(s) interactor B Identification method participant A Identification method participant B uniprotkb:Q9RA63 uniprotkb:Q9RA63 intact:EBI-7698530|ensemblbacteria:BAD71310|uniprotkb:P74942|intact:MINT-1131158|uniprotkb:Q5SI87 intact:EBI-7698530|ensemblbacteria:BAD71310|uniprotkb:P74942|intact:MINT-1131158|uniprotkb:Q5SI87 psi-mi:clpb_thet8(display_long)|uniprotkb:clpB(gene name)|psi-mi:clpB(display_short)|uniprotkb:TTHA1487(locus name) psi-mi:clpb_thet8(display_long)|uniprotkb:clpB(gene name)|psi-mi:clpB(display_short)|uniprotkb:TTHA1487(locus name) psi-mi:"MI:0071"(molecular sieving) Yamasaki et al. (2011) mint:MINT-8174905|pubmed:21554542|imex:IM-16726|mint:fj-11-0194.r1 taxid:300852(thet8)|taxid:300852("Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)") taxid:300852(thet8)|taxid:300852("Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)") psi-mi:"MI:0407"(direct interaction) psi-mi:"MI:0471"(MINT) intact:EBI-8663742|mint:MINT-8174910|imex:IM-16726-1 - - psi-mi:"MI:0499"(unspecified role) psi-mi:"MI:0499"(unspecified role) psi-mi:"MI:0497"(neutral component) psi-mi:"MI:0497"(neutral component) psi-mi:"MI:0326"(protein) psi-mi:"MI:0326"(protein) ensemblbacteria:BAD71310(gene)|ensemblbacteria:BAD71310(transcript)|go:"GO:0005524"(ATP binding)|go:"GO:0005737"(cytoplasm)|go:"GO:0009408"(response to heat)|go:"GO:0042026"(protein refolding)|go:"GO:0042802"(identical protein binding)|interpro:IPR001270(Chaperonin clpA/B)|interpro:IPR003593(AAA+ ATPase, core)|interpro:IPR003959(AAA ATPase, core)|interpro:IPR004176(Clp, N-terminal)|interpro:IPR017730(Chaperonin ClpB)|interpro:IPR018368|interpro:IPR019489|interpro:IPR027417|interpro:IPR028299|interpro:IPR036628|interpro:IPR041546|rcsb pdb:1QVR|rcsb pdb:4FCT|rcsb pdb:4FCV|rcsb pdb:4FCW|rcsb pdb:4HSE|rcsb pdb:4LJ4|rcsb pdb:4LJ5|rcsb pdb:4LJ6|rcsb pdb:4LJ7|rcsb pdb:4LJ8|rcsb pdb:4LJ9|rcsb pdb:4LJA|rcsb pdb:4FD2|refseq:YP_144753.1|refseq:WP_011228712.1|dip:DIP-41758N|mint:MINT-8174912(identity) ensemblbacteria:BAD71310(gene)|ensemblbacteria:BAD71310(transcript)|go:"GO:0005524"(ATP binding)|go:"GO:0005737"(cytoplasm)|go:"GO:0009408"(response to heat)|go:"GO:0042026"(protein refolding)|go:"GO:0042802"(identical protein binding)|interpro:IPR001270(Chaperonin clpA/B)|interpro:IPR003593(AAA+ ATPase, core)|interpro:IPR003959(AAA ATPase, core)|interpro:IPR004176(Clp, N-terminal)|interpro:IPR017730(Chaperonin ClpB)|interpro:IPR018368|interpro:IPR019489|interpro:IPR027417|interpro:IPR028299|interpro:IPR036628|interpro:IPR041546|rcsb pdb:1QVR|rcsb pdb:4FCT|rcsb pdb:4FCV|rcsb pdb:4FCW|rcsb pdb:4HSE|rcsb pdb:4LJ4|rcsb pdb:4LJ5|rcsb pdb:4LJ6|rcsb pdb:4LJ7|rcsb pdb:4LJ8|rcsb pdb:4LJ9|rcsb pdb:4LJA|rcsb pdb:4FD2|refseq:YP_144753.1|refseq:WP_011228712.1|dip:DIP-41758N|mint:MINT-8174912(identity) - comment:mint|function:Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Acts before dnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of clpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by dnaK|comment:"Stoichiometry: 6.0" comment:mint|function:Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Acts before dnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of clpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by dnaK|comment:"Stoichiometry: 6.0" figure legend:f6|comment:mint|full coverage:Only protein-protein interactions|curation depth:imex curation taxid:-1(in vitro)|taxid:-1(In vitro) - 2011/05/05 2014/10/16 rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852 rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852 intact-crc:FCAA2D2058CF90F1|rigid:1kYSt+M7CxT2TpWup5x5PcejORs false mutation decreasing interaction:322-322(MINT-8174916) mutation decreasing interaction:322-322(MINT-8174916) 6 0 psi-mi:"MI:0396"(predetermined participant) psi-mi:"MI:0396"(predetermined participant) uniprotkb:Q9RA63 uniprotkb:Q9RA63 intact:EBI-7698530|ensemblbacteria:BAD71310|uniprotkb:P74942|intact:MINT-1131158|uniprotkb:Q5SI87 intact:EBI-7698530|ensemblbacteria:BAD71310|uniprotkb:P74942|intact:MINT-1131158|uniprotkb:Q5SI87 psi-mi:clpb_thet8(display_long)|uniprotkb:clpB(gene name)|psi-mi:clpB(display_short)|uniprotkb:TTHA1487(locus name) psi-mi:clpb_thet8(display_long)|uniprotkb:clpB(gene name)|psi-mi:clpB(display_short)|uniprotkb:TTHA1487(locus name) psi-mi:"MI:0071"(molecular sieving) Yamasaki et al. (2011) mint:MINT-8174905|pubmed:21554542|imex:IM-16726|mint:fj-11-0194.r1 taxid:300852(thet8)|taxid:300852("Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)") taxid:300852(thet8)|taxid:300852("Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)") psi-mi:"MI:0407"(direct interaction) psi-mi:"MI:0471"(MINT) intact:EBI-8663756|mint:MINT-8174921|imex:IM-16726-2 - - psi-mi:"MI:0499"(unspecified role) psi-mi:"MI:0499"(unspecified role) psi-mi:"MI:0497"(neutral component) psi-mi:"MI:0497"(neutral component) psi-mi:"MI:0326"(protein) psi-mi:"MI:0326"(protein) ensemblbacteria:BAD71310(gene)|ensemblbacteria:BAD71310(transcript)|go:"GO:0005524"(ATP binding)|go:"GO:0005737"(cytoplasm)|go:"GO:0009408"(response to heat)|go:"GO:0042026"(protein refolding)|go:"GO:0042802"(identical protein binding)|interpro:IPR001270(Chaperonin clpA/B)|interpro:IPR003593(AAA+ ATPase, core)|interpro:IPR003959(AAA ATPase, core)|interpro:IPR004176(Clp, N-terminal)|interpro:IPR017730(Chaperonin ClpB)|interpro:IPR018368|interpro:IPR019489|interpro:IPR027417|interpro:IPR028299|interpro:IPR036628|interpro:IPR041546|rcsb pdb:1QVR|rcsb pdb:4FCT|rcsb pdb:4FCV|rcsb pdb:4FCW|rcsb pdb:4HSE|rcsb pdb:4LJ4|rcsb pdb:4LJ5|rcsb pdb:4LJ6|rcsb pdb:4LJ7|rcsb pdb:4LJ8|rcsb pdb:4LJ9|rcsb pdb:4LJA|rcsb pdb:4FD2|refseq:YP_144753.1|refseq:WP_011228712.1|dip:DIP-41758N|mint:MINT-8174923(identity) ensemblbacteria:BAD71310(gene)|ensemblbacteria:BAD71310(transcript)|go:"GO:0005524"(ATP binding)|go:"GO:0005737"(cytoplasm)|go:"GO:0009408"(response to heat)|go:"GO:0042026"(protein refolding)|go:"GO:0042802"(identical protein binding)|interpro:IPR001270(Chaperonin clpA/B)|interpro:IPR003593(AAA+ ATPase, core)|interpro:IPR003959(AAA ATPase, core)|interpro:IPR004176(Clp, N-terminal)|interpro:IPR017730(Chaperonin ClpB)|interpro:IPR018368|interpro:IPR019489|interpro:IPR027417|interpro:IPR028299|interpro:IPR036628|interpro:IPR041546|rcsb pdb:1QVR|rcsb pdb:4FCT|rcsb pdb:4FCV|rcsb pdb:4FCW|rcsb pdb:4HSE|rcsb pdb:4LJ4|rcsb pdb:4LJ5|rcsb pdb:4LJ6|rcsb pdb:4LJ7|rcsb pdb:4LJ8|rcsb pdb:4LJ9|rcsb pdb:4LJA|rcsb pdb:4FD2|refseq:YP_144753.1|refseq:WP_011228712.1|dip:DIP-41758N|mint:MINT-8174923(identity) - comment:mint|function:Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Acts before dnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of clpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by dnaK|comment:"Stoichiometry: 6.0" comment:mint|function:Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Acts before dnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of clpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by dnaK|comment:"Stoichiometry: 6.0" figure legend:f6|comment:mint|full coverage:Only protein-protein interactions|curation depth:imex curation taxid:-1(in vitro)|taxid:-1(In vitro) - 2011/05/05 2014/10/16 rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852 rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852 intact-crc:70643F6A3EC284C1|rigid:1kYSt+M7CxT2TpWup5x5PcejORs false mutation decreasing interaction:323-323(MINT-8174924) mutation decreasing interaction:323-323(MINT-8174924) 6 0 psi-mi:"MI:0396"(predetermined participant) psi-mi:"MI:0396"(predetermined participant)