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dnaK | Chaperone Hsp70; Acts as a chaperone. (638 aa) | ||||
dnaJ | Heat shock 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, [...] (379 aa) | ||||
STM0402 | Similar to E. coli alkyl hydroperoxide reductase, C22 subunit; detoxification of hydroperoxides (AAC73706.1); Blastp hit to AAC73706.1 (187 aa), 36% identity in aa 1 - 186. (200 aa) | ||||
clpP | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (207 aa) | ||||
clpX | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (423 aa) | ||||
lon | DNA-binding protein; 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. (784 aa) | ||||
htpG | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. (632 aa) | ||||
ybbN | Similar to E. coli putative thioredoxin-like protein (AAC73594.1); Blastp hit to AAC73594.1 (296 aa), 94% identity in aa 13 - 296. (284 aa) | ||||
ahpC | Alkyl hydroperoxide reductase, C22 subunit; 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. (187 aa) | ||||
ahpF | Alkyl hydroperoxide reductase, F52a subunit; Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. (521 aa) | ||||
grxA | Redox coenzyme for glutathione-dependent ribonucleotide reductase glutaredoxin1; The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase (By similarity); Belongs to the glutaredoxin family. (87 aa) | ||||
yljA | Putative cytoplasmic protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. (106 aa) | ||||
clpA | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. (758 aa) | ||||
trxB | Similar to E. coli thioredoxin reductase (AAC73974.1); Blastp hit to AAC73974.1 (321 aa), 96% identity in aa 1 - 320. (322 aa) | ||||
sodC | Gifsy-2 prophage superoxide dismutase precursor (Cu-Zn); Destroys radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the Cu-Zn superoxide dismutase family. (177 aa) | ||||
katE | Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide. (750 aa) | ||||
sodB | Iron superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family. (193 aa) | ||||
sodC-2 | Copper/zinc superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the Cu-Zn superoxide dismutase family. (173 aa) | ||||
ychJ | Putative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC74315.1); Blastp hit to AAC74315.1 (152 aa), 78% identity in aa 1 - 152; Belongs to the UPF0225 family. (152 aa) | ||||
trxC | Similar to E. coli putative thioredoxin-like protein (AAC75635.1); Blastp hit to AAC75635.1 (139 aa), 94% identity in aa 1 - 139; Belongs to the thioredoxin family. (139 aa) | ||||
clpB | ATP-dependent protease; 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). Required for colonization of the gastroi [...] (857 aa) | ||||
grpE | Molecular chaparone; 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-depe [...] (196 aa) | ||||
STM2682 | Putative cytoplasmic protein. (64 aa) | ||||
STM2804 | Putative cytoplasmic protein; Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity. Belongs to the AhpD family. (143 aa) | ||||
yrfH | Heat shock protein; Predicted small RNA-binding protein; similar to E. coli orf, hypothetical protein (AAC76425.1); Blastp hit to AAC76425.1 (133 aa), 95% identity in aa 1 - 133; Belongs to the HSP15 family. (133 aa) | ||||
yrfI | Heat shock protein 33; 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. (294 aa) | ||||
ibpB | Small heat shock protein; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. (142 aa) | ||||
ibpA | Small heat shock protein; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. (137 aa) | ||||
trxA | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family. (109 aa) | ||||
sodA | Superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family. (206 aa) | ||||
hslU | ATPase component of the HslUV protease; 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. (443 aa) | ||||
hslV | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. Belongs to the peptidase T1B family. HslV subfamily. (176 aa) | ||||
katG | Catalase; Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity; Belongs to the peroxidase family. Peroxidase/catalase subfamily. (726 aa) | ||||
oxyR | Regulatory protein sensor for oxidative stress; Regulates intracellular hydrogen peroxide (LysR family); similar to E. coli activator, hydrogen peroxide-inducible genes (AAC76943.1); Blastp hit to AAC76943.1 (305 aa), 95% identity in aa 1 - 305; Belongs to the LysR transcriptional regulatory family. (305 aa) | ||||
soxS | Transcriptional activator of superoxide response regulon; Transcriptional activator of the superoxide response regulon of E.coli that includes at least 10 genes such as sodA, nfo, zwf and micF. Binds the DNA sequence 5'-GCACN(7)CAA-3'. It also facilitates the subsequent binding of RNA polymerase to the micF and the nfo promoters (By similarity). (107 aa) | ||||
soxR | Redox-sensing transcriptional activator SoxR; Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron- sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress (By similarity). (152 aa) | ||||
mopB | Chaperone Hsp10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (97 aa) | ||||
mopA | Chaperone Hsp60 with peptide-dependent ATPase activity; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa) |