ATP-dependent hsl protease ATP-binding subunit hslU; 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.

Heat shock protein (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 [...]

ATPase and specificity subunit of ClpA-ClpP ATP-dependent serine protease, chaperone activity; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the ClpA/ClpB family.

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

Putative heat shock protein (HSP-70 COFACTOR), grpE; 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 c [...]

Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity.

ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.

Putative lysophospholipase L2 (pldB-like); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.

Putative molecular chaperone, heat shock Hsp20 family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor; Belongs to the small heat shock protein (HSP20) family.