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.

Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...]

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 [...]

Putative chaperone protein dnaJ. homology to dnaJ of E. coli of 32% (sprot|DNAJ_ECOLI) Acts as a co-chaperone. Stimulates jointly with grpE the ATPase activity of dnaK (By similarity). Pfam: DnaJ domain, DnaJ central domain (4 repeats), DnaJ Cterminal region no singal peptide no TMHs; Family membership.

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

Putative small heat shock protein. Homology to hsp18 of C. acetobutylicum of 35% (sprot|HS18_CLOAB) InterPro: Heat shock hsp20 (alpha crystallin) proteins family (IPR002068) Pfam: Hsp20/alpa cystallin family no signal peptide no TMHs; Function unclear.

Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership.

Probable chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.