GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...]

Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023: IPR 013126: IPR 018181; KEGG: phe:Phep_3231 Fe-S protein assembly chaperone HscA; PFAM: Heat shock protein 70; SPTR: Heat shock protein 70; PFAM: Hsp70 protein; TIGRFAM: Fe-S protein assembly chaperone HscA.

Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.

Heat shock protein Hsp90; COGs: COG0326 Molecular chaperone HSP90 family; InterPro IPR001404: IPR 003594: IPR 020576: IPR 020575; KEGG: phe:Phep_0051 heat shock protein 90; PFAM: Heat shock protein Hsp90-like; ATP-binding region ATPase domain protein; SPTR: Heat shock protein Hsp90; PFAM: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; Hsp90 protein.

Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

LSU ribosomal protein L12P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family.

ATP-dependent chaperone ClpB; 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; Belongs to the ClpA/ClpB family.

ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterPro IPR001270: IPR 004176: IPR 003959: IPR 001943: IPR 013093: IPR 019489: IPR 018368: IPR 003593; KEGG: phe:Phep_1132 ATPase AAA-2 domain protein; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATP-dependent Clp protease, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; UvrB/uvrC motif; ATPase family asso [...]

Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]