Chaperone Hsp60 with peptide-dependent ATPase activity; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Chaperone Hsp10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

Similar to E. coli putative heat shock protein (AAC75130.1); Blastp hit to AAC75130.1 (471 aa), 88% identity in aa 22 - 471.

Putative heatshock protein, homolog of hsp70 in Hsc66 subfamily; Similar to E. coli putative dnaK protein (AAC73751.1); Blastp hit to AAC73751.1 (556 aa), 83% identity in aa 1 - 556; Belongs to the heat shock protein 70 family.

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. Involved in the maturation of IscU.

Heat shock 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, [...]

Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.

ATPase component of the HslUV protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.

Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. Belongs to the peptidase T1B family. HslV subfamily.