Transcriptional regulator for aaeXAB operon; Activates transcription of the aaeXAB operon.

Quorum sensing DNA-binding response regulator in two-component regulatory system with QseC; Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. Currently it is not known whether this effect is direct or not.

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

Fumarate hydratase (fumarase A), aerobic Class I; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate.

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

Fumarate hydratase (fumarase C),aerobic Class II; Involved in the TCA cycle. FumC seems to be a backup enzyme for FumA under conditions of iron limitation and oxidative stress. Catalyzes the stereospecific interconversion of fumarate to L-malate. Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

Malate dehydrogenase, NAD(P)-binding; Catalyzes the reversible oxidation of malate to oxaloacetate.

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

NADH:ubiquinone oxidoreductase, fused CD subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family.

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

Glucosephosphate isomerase; Protein involved in glycolysis and gluconeogenesis; Belongs to the GPI family.

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

Succinate dehydrogenase, flavoprotein subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

Succinate dehydrogenase, FeS subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

Succinate dehydrogenase, membrane subunit, binds cytochrome b556; Membrane-anchoring subunit of succinate dehydrogenase (SDH); Belongs to the cytochrome b560 family.

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

succinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. Can use either ATP or GTP, but prefers ATP. It can also function in the other direction for anabolic purposes, and this may be particularly impor [...]

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

succinyl-CoA synthetase, NAD(P)-binding, alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. Can use either ATP or GTP, but prefers ATP. It can also function in the other direction for anabolic purposes, and this may be particularly importan [...]

Carbamoyl-phosphate synthase large subunit; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process; Belongs to the CarB family.

Chaperone Hsp40, DnaK co-chaperone; Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. 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 t [...]

Carbamoyl-phosphate synthase large subunit; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process; Belongs to the CarB family.

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 [...]

Carbamoyl-phosphate synthase large subunit; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process; Belongs to the CarB family.

Dihydro-orotate oxidase, FMN-linked; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

Carbamoyl-phosphate synthase large subunit; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process; Belongs to the CarB family.

Orotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP); Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.

Carbamoyl-phosphate synthase large subunit; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process; Belongs to the CarB family.

Orotidine-5'-phosphate decarboxylase; Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).

Carbamoyl-phosphate synthase large subunit; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process; Belongs to the CarB family.

RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded 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. [...]

Chaperone Hsp40, DnaK co-chaperone; Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. 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 t [...]

Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded 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. [...]

Chaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.