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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) | ||||
rpoE | Sigma E (sigma 24) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). (191 aa) | ||||
yegD | Similar to E. coli putative heat shock protein (AAC75130.1); Blastp hit to AAC75130.1 (471 aa), 88% identity in aa 22 - 471. (450 aa) | ||||
sbmC | DNA gyrase inhibitor; Inhibits the supercoiling activity of DNA gyrase. Acts by inhibiting DNA gyrase at an early step, prior to (or at the step of) binding of DNA by the gyrase. It protects cells against toxins that target DNA gyrase, by inhibiting activity of these toxins and reducing the formation of lethal double-strand breaks in the cell. (155 aa) | ||||
cspB | Putative cold-shock protein; Similar to E. coli cold shock-like protein (AAC74625.1); Blastp hit to AAC74625.1 (70 aa), 84% identity in aa 1 - 70. (70 aa) | ||||
hnr | Response regulator in protein turnover; Regulates the turnover of the sigma S factor (RpoS) by promoting its proteolysis in exponentially growing cells. Acts by binding and delivering RpoS to the ClpXP protease. RssB is not co- degraded with RpoS, but is released from the complex and can initiate a new cycle of RpoS recognition and degradation. (337 aa) | ||||
hslJ | Similar to E. coli heat shock protein hslJ (AAC74461.1); Blastp hit to AAC74461.1 (140 aa), 69% identity in aa 1 - 138. (136 aa) | ||||
STM1251 | Putative molecular chaperone (small heat shock protein); Similar to E. coli heat shock protein (AAC76710.1); Blastp hit to AAC76710.1 (137 aa), 33% identity in aa 1 - 136; Belongs to the small heat shock protein (HSP20) family. (155 aa) | ||||
iraM | Putative cytoplasmic protein; Involved in the stabilization of the sigma stress factor RpoS; Belongs to the IraM/RssC family. (120 aa) | ||||
yccV | Putative inner membrane protein; Involved in the degradation of certain denaturated proteins, including DnaA, during heat shock stress; Belongs to the HspQ family. (105 aa) | ||||
htpG | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. (632 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) | ||||
rpoS | Sigma S (sigma 38) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response. (330 aa) | ||||
iraD | Putative cytoplasmic protein; Inhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS during oxidative stress. Its effect on RpoS stability is due to its interaction with RssB, which probably blocks the interaction of RssB with RpoS, and the consequent delivery of the RssB-RpoS complex to the ClpXP protein degradation pathway. (126 aa) | ||||
deaD | Cysteine sulfinate desulfinase; DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation. (646 aa) | ||||
degQ | Similar to E. coli serine endoprotease (AAC76266.1); Blastp hit to AAC76266.1 (455 aa), 89% identity in aa 1 - 455; Belongs to the peptidase S1C family. (455 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) | ||||
hfq | Host factor I for bacteriophage Q beta replication; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs (By similarity). Plays a central regulatory role in the microbial response to space flight conditions. Is essential for virulence and is required for efficient invasion of non-phagocytic cells. (102 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) | ||||
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) | ||||
yihE | Putative homoserine kinase type II; A protein kinase that (auto)phosphorylates on Ser and Thr residues, probably involved in the extracytoplasmic stress response. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species (By similarity). (328 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) | ||||
cspA | Major cold shock protein 7.4; Binds to and stimulates the transcription of the CCAAT- containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3' (By similarity). (70 aa) | ||||
rpoH | Sigma H factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. (284 aa) | ||||
ompR | Response regulator in two-component regulatory system with EnvZ; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). Plays a central role in both acid and osmotic stress responses. Binds to the promoter of both ompC and ompF; at low osmolarity it activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity). (239 aa) | ||||
envZ | Sensory histidine kinase in two-component regulatory system with OmpR; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). EnvZ functions as a membrane- associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolarity OmpR activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity). (450 aa) | ||||
thiJ | 4-methyl-5(beta-hydroxyethyl)-thiazole synthesis; Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, collagen, g [...] (196 aa) | ||||
yaiB | Putative cytoplasmic protein; Inhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS especially during phosphate and magnesium starvation, but also in stationary phase and during nitrogen starvation. Its effect on RpoS stability is due to its interaction with RssB, which probably blocks the interaction of RssB with RpoS, and the consequent delivery of the RssB-RpoS complex to the ClpXP protein degradation pathway. Belongs to the IraP family. (88 aa) | ||||
yaiV | Putative inner membrane protein; Involved in oxidative stress resistance. (207 aa) | ||||
phoE | Outer membrane pore protein e (e,ic,nmpab); Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes; Belongs to the Gram-negative porin family. (350 aa) | ||||
radA | Putative ATP-dependent protease; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. Belongs to the RecA family. RadA subfamily. (460 aa) | ||||
ytfE | Putative cell morphogenesis; Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions. (220 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) | ||||
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) | ||||
htrA | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] (475 aa) |