ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associated with various cellular activities (AAA); UvrB/uvrC motif; Belongs to the ClpA/ClpB family.

Molecular chaperone GrpE (heat shock 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. [...]

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

ATP dependent peptidase CodWX, CodW component; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.

PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp domain.

ATP-dependent protease HslVU, ATPase subunit; 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.

PFAM: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.

Molecular chaperone of HSP90 family; Molecular chaperone. Has ATPase activity.