DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell 2003 imex curation Lee S., Sowa ME., Watanabe YH., Sigler PB., Chiu W., Yoshida M., Tsai FT. ftsai@bcm.tmc.edu Only protein-protein interactions imex curation thet8 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Lee S., Sowa ME., Watanabe YH., Sigler PB., Chiu W., Yoshida M., Tsai FT. ftsai@bcm.tmc.edu Accepted 2021-OCT-05 AT 13:04 BST AT 13:04 BST by ORCHARD Cell 2003 imex curation clpb_thet8 Chaperone protein ClpB clpB TTHA1487 protein protein thet8 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) MNLERWTQAAREALAQAQVLAQRMKHQAIDLPHLWAVLLKDERSLAWRLLEKAGADPKALKELQERELARLPKVEGAEVGQYLTSRLSGALNRAEALMEELKDRYVAVDTLVLALAEATPGLPGLEALKGALKELRGGRTVQTEHAESTYNALEQYGIDLTRLAAEGKLDPVIGRDEEIRRVIQILLRRTKNNPVLIGEPGVGKTAIVEGLAQRIVKGDVPEGLKGKRIVSLQMGSLLAGAKYRGEFEERLKAVIQEVVQSQGEVILFIDELHTVVGAGKAEGAVDAGNMLKPALARGELRLIGATTLDEYREIEKDPALERRFQPVYVDEPTVEETISILRGLKEKYEVHHGVRISDSAIIAAATLSHRYITERRLPDKAIDLIDEAAARLRMALESAPEEIDALERKKLQLEIEREALKKEKDPDSQERLKAIEAEIAKLTEEIAKLRAEWEREREILRKLREAQHRLDEVRREIELAERQYDLNRAAELRYGELPKLEAEVEALSEKLRGARFVRLEVTEEDIAEIVSRWTGIPVSKLLEGEREKLLRLEEELHKRVVGQDEAIRAVADAIRRARAGLKDPNRPIGSFLFLGPTGVGKTELAKTLAATLFDTEEAMIRIDMTEYMEKHAVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVILFDEIEKAHPDVFNILLQILDDGRLTDSHGRTVDFRNTVIILTSNLGSPLILEGLQKGWPYERIRDEVFKVLQQHFRPEFLNRLDEIVVFRPLTKEQIRQIVEIQLSYLRARLAEKRISLELTEAAKDFLAERGYDPVFGARPLRRVIQRELETPLAQKILAGEVKEGDRVQVDVGPAGLVFAVPARVEA DIP protein Q9RA63 original sequence version: 92 mint 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 FB9A39BB040363E0 clpb-11 1 2 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig 2, Table 1