Thiol:disulfide interchange protein precursor; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily.

Thioredoxin reductase.

Methionine sulfoxide reductase A; 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.

Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen.

Alkyl hydroperoxide reductase subunit C; 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.

Putative mercuric reductase; Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Chaperone Hsp40; 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, DnaK and [...]

Cytochrome o ubiquinol oxidase subunit II.