Heat shock response protein.

Alkyl hydroperoxide reductase peroxiredoxin component AhpC; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.

Heat shock response protein.

ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family.

Heat shock response protein.

Stress-induced multi-chaperone system component ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to [...]

Heat shock response protein.

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 [...]

Heat shock response protein.

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

Heat shock response protein.

Glutathione-disulfide reductase Gor.

Heat shock response protein.

60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Heat shock response protein.

10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

Heat shock response protein.

Heat shock nucleotide exchange factor 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 cycle. Sev [...]

Heat shock response protein.

Redox regulated chaperone HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.

Heat shock response protein.

HlsVU protease ATPase component 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 response protein.

HlsVU protease peptidase component HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.

Heat shock response protein.

Heat shock chaperone HtpG; Molecular chaperone. Has ATPase activity.

Heat shock response protein.

ATP-dependent protease La Lon; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.

Heat shock response protein.

Oligopeptidase A PrlC.

Heat shock response protein.

Thioredoxin reductase TrxB.

Heat shock response protein.

Peroxiredoxin TsaA.

DnaJ domain protein.

ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family.

DnaJ domain protein.

Stress-induced multi-chaperone system component ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to [...]

DnaJ domain protein.

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