ATP dependent Clp protease proteolytic subunit 2; 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 (By similarity). Probably partially responsible for degradation of ECF sigma factor SigR prime; Belongs to the peptidase S14 family.

Putative ATP-dependent Clp protease; Has lost one of the conserved residue (Ser) proposed to be part of the active site. Therefore it could be inactive.

Putative ATP-dependent Clp protease proteolytic subunit 2; Has lost one of the conserved residue (His) proposed to be part of the active site. Therefore it could be inactive.

SC3C8.27c, clpA, probable clp protease ATP binding subunit, len: 842 aa; highly similar to many e.g. CLPB_ECOLI clpB protein (857 aa), fasta scores; opt: 975 z-score: 1914.6 E(): 0, 46.8% identity in 857 aa overlap anCLAB_LYCES ATP-dependent clp protease atp-binding subunit (923 aa), fasta scores; opt: 2335 z-score: 2174.3 E(): 0, 50.3% identity in 758 aa overlap. Contains 2x PS00017 ATP/GTP-binding site motif A (P-loop), PS00870 and PS00871 Chaperonins clpA/B signatures 1 and 2, Pfam match to entry clpA_B PF00495, Chaperonins clpA/B, score 1127.99 and probable coiled-coil from aa 432 [...]

Putative cell division trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily.

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

ATP-dependent protease ATP-binding subunit; 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 (By similarity). Belongs to the ClpA/ [...]

60 kD chaperonin cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Heat chock 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-depen [...]