Trifunctional thioredoxin/methionine sulfoxide reductase A/B protein; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.

tRNA threonylcarbamoyladenosine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.

Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.

Glycine dehydrogenase (aminomethyl-transferring); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.

DNA starvation/stationary phase protection protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Dps family.

Ribosomal subunit interface protein; Derived by automated computational analysis using gene prediction method: Protein Homology.

Molecular chaperone 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, [...]