MALATE SYNTHASE; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily.

METHYLCITRATE SYNTHASE; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity.

MALATE SYNTHASE; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily.

PYRUVATE CARBOXYLASE; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.

PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); 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). Necessary [...]

Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.

PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); 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). Necessary [...]

60 KDA CHAPERONIN (PROTEIN CPN60) (GROEL PROTEIN) C-terminal fragment; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); 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). Necessary [...]

Chaperonin cpn60 (60Kd subunit); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); 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). Necessary [...]

TRANSCRIPTIONAL REGULATOR MERR FAMILY.

PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); 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). Necessary [...]

RNA POLYMERASE SIGMA FACTOR; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.

PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); 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). Necessary [...]

PUTATIVE RNA POLYMERASE SIGMA FACTOR, ECF family; Belongs to the sigma-70 factor family. ECF subfamily.

PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); 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). Necessary [...]

RNA POLYMERASE SIGMA-70 FACTOR, ECF SUBFAMILY.

Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.

PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); 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). Necessary [...]

Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.

60 KDA CHAPERONIN (PROTEIN CPN60) (GROEL PROTEIN) C-terminal fragment; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.

Chaperonin cpn60 (60Kd subunit); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.

TRANSCRIPTIONAL REGULATOR MERR FAMILY.

Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.

50S RIBOSOMAL PROTEIN L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.

Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.

50S RIBOSOMAL PROTEIN L10; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family.

Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.

RNA POLYMERASE SIGMA FACTOR; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.

Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.

PUTATIVE RNA POLYMERASE SIGMA FACTOR, ECF family; Belongs to the sigma-70 factor family. ECF subfamily.

60 KDA CHAPERONIN (PROTEIN CPN60) (GROEL PROTEIN) C-terminal fragment; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); 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). Necessary [...]

60 KDA CHAPERONIN (PROTEIN CPN60) (GROEL PROTEIN) C-terminal fragment; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.

60 KDA CHAPERONIN (PROTEIN CPN60) (GROEL PROTEIN) C-terminal fragment; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Chaperonin cpn60 (60Kd subunit); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.