Peptide methionine sulfoxide reductase msrA; 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.

Peptide methionine sulphoxide reductase reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide to methionine. MsrA is specific for methionine-S-sulfoxides. Though their active sites show approximate mirror symmetry, MsrA and MsrB are structurally unrelated. In each case, conserved amino acid motifs mediate the stereo-specific recognition and reduction of the substrate. Thioredoxin acts as a cofactor. Localized in the cytoplasm; High confidence in function and specificity.

Conserved hypothetical protein; Contains two transmembrane segments; Localized in the cytoplasmic membrane.

Alginate lyase, family PL7; Modular protein with a N-terminal carbohydrate binding module of the family 32 (CBM32) and a C-terminal alginate lyase domain of the family 7 of the polysaccharide lyases (PL7). Alginate lyase catalyzes the eliminative cleavage of polysaccharides containing beta-D- mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their ends. Features a signal peptide cleaved between residues 34 and 35. Likely localized in the outer membrane; High confidence in function and specificity.

Protein that contains in the N-terminal part, one cadherin like domain and in its C-terminal part, five PKD repeats. The PKD domains are present in the extracellular parts of proteins involved in interactions with other proteins or polysaccharides; Signal peptide cleaved between the residues 19 and 20; Putatively localized in the outer membrane.