ATP-dependent CLP protease ATP-binding subunit; Similar to Escherichia coli, Escherichia coli O6, and Escherichia coli O157:H7 ATP-dependent Clp protease ATP-binding subunit ClpA or LopD or b0882 or c1019 or z1119 or ecs0968 SWALL:CLPA_ECOLI (SWALL:P15716) (758 aa) fasta scores: E(): 0, 90.23% id in 758 aa; Belongs to the ClpA/ClpB family.

Putative chaperone; Similar to Thermus thermophilus ClpB protein ClpB SWALL:CLPB_THETH (SWALL:Q9RA63) (854 aa) fasta scores: E(): 7e-69, 37.97% id in 869 aa, and to Yersinia pestis clp ATPase ClpB2 or ypo3599 or ClpB or y0275 SWALL:Q8ZB30 (EMBL:AJ414157) (867 aa) fasta scores: E(): 6.3e-209, 68.66% id in 868 aa; Belongs to the ClpA/ClpB family.

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

Chaperone protein; Molecular chaperone. Has ATPase activity.

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. Several rounds of ATP-depen [...]

ATP-dependent Hsl protease ATP-binding subunit (heat shock protein); 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.

Chaperone protein DnaK; Acts as a chaperone; 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.

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 [...]