#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:0114"(x-ray crystallography)	Biter et al. (2012)	pubmed:22802670|doi:10.1073/pnas.1207040109|imex:IM-20694	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:0465"(DIP)	intact:EBI-15999786|imex:IM-20694-1|dip:DIP-190340E	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	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	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	psi-mi:"MI:0465"(dip)	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: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	full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:562(ecolx)|taxid:562(Escherichia coli)	-	2017/08/07	2017/08/10	rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852	rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852	rigid:1kYSt+M7CxT2TpWup5x5PcejORs	false	sufficient binding region:542-854	sufficient binding region:542-854	-	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:0030"(cross-linking study)	Biter et al. (2012)	pubmed:22802670|doi:10.1073/pnas.1207040109|imex:IM-20694	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:0465"(DIP)	intact:EBI-15999804|imex:IM-20694-2|dip:DIP-190340E	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	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	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	psi-mi:"MI:0465"(dip)	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: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	full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:562(ecolx)|taxid:562(Escherichia coli)	-	2017/08/07	2017/08/10	rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852	rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852	rigid:1kYSt+M7CxT2TpWup5x5PcejORs	false	mutation:810-810,746-746	mutation:810-810,746-746	-	0	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)
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)	Biter et al. (2012)	pubmed:22802670|doi:10.1073/pnas.1207040109|imex:IM-20694	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:0465"(DIP)	intact:EBI-15999824|imex:IM-20694-3|dip:DIP-190340E	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	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	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	psi-mi:"MI:0465"(dip)	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: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	full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:562(ecolx)|taxid:562(Escherichia coli)	-	2017/08/07	2017/08/10	rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852	rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852	rigid:1kYSt+M7CxT2TpWup5x5PcejORs	false	-	-	-	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:0030"(cross-linking study)	Biter et al. (2012)	pubmed:22802670|doi:10.1073/pnas.1207040109|imex:IM-20694	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:0465"(DIP)	intact:EBI-15999840|imex:IM-20694-4|dip:DIP-190340E	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	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	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	psi-mi:"MI:0465"(dip)	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: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	full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:562(ecolx)|taxid:562(Escherichia coli)	-	2017/08/07	2017/08/10	rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852	rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852	rigid:1kYSt+M7CxT2TpWup5x5PcejORs	false	mutation:821-821,576-576	mutation:821-821,576-576	-	0	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)
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:0030"(cross-linking study)	Biter et al. (2012)	pubmed:22802670|doi:10.1073/pnas.1207040109|imex:IM-20694	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:0465"(DIP)	intact:EBI-15999860|imex:IM-20694-5|dip:DIP-190340E	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	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	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	psi-mi:"MI:0465"(dip)	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: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	full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:562(ecolx)|taxid:562(Escherichia coli)	-	2017/08/07	2017/08/10	rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852	rogid:fBC0qwrN9N1uSxpfr7eQ7KRJugM300852	rigid:1kYSt+M7CxT2TpWup5x5PcejORs	false	mutation:776-776,581-581	mutation:776-776,581-581	-	0	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)	psi-mi:"MI:0818"(molecular weight estimation by coomasie staining)