Chaperone Hsp70, co-chaperone with DnaJ; Acts as a chaperone; Belongs to the heat shock protein 70 family.

DnaK-like molecular chaperone specific for IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.

Putative Molecular chaperone; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor.

Cobalt-nickel-resistance system transmembrane protein; Function of strongly homologous gene; transporter.

Putative site-specific recombinase, resolvase family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.

Cpn60 chaperonin GroEL, large subunit of GroESL(Chaperonin Cpn60/TCP-1,23-525); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

DnaJ-class molecular chaperone; Function of strongly homologous gene; factor.

Conserved protein of unknown function（DnaJ N-terminal domain-containing protein） Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure.

Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...]