DsbB (UniProt ID: Q1H058) belongs to the disulfide oxidoreductase family and operates in the bacterial periplasm. In M. flagellatus, it is encoded by the dsbB gene (locus tag: Mfla_1862) and expressed as a 166-amino-acid protein with a predicted molecular weight of ~18.5 kDa (calculated from sequence data) .
DsbB acts as a redox transducer, transferring electrons from the periplasmic oxidoreductase DsbA to membrane-bound quinones (e.g., ubiquinone). This cycle ensures DsbA remains oxidized, enabling it to catalyze disulfide bond formation in substrate proteins .
The recombinant form (rDsbB) is produced in E. coli systems for biochemical studies. Key production details include:
| Parameter | Detail |
|---|---|
| Expression system | E. coli (optimized codon usage) |
| Tag | Undisclosed (determined during production) |
| Storage | Tris buffer, 50% glycerol; stable at -20°C or -80°C |
| Purity | >90% (SDS-PAGE verified) |
Amino acids 1–166 (full-length).
Conserved motifs: CXXC (residues 41–44, 104–107) and transmembrane domains (residues 15–37, 50–72, etc.) .
DsbB’s role in M. flagellatus is indirectly linked to its methylotrophic metabolism:
Metabolic redundancy: M. flagellatus employs parallel pathways for formaldehyde oxidation (cyclic vs. linear). DsbB likely stabilizes enzymes like 6-phosphogluconate dehydrogenase (GndA/B), which are critical for the cyclic pathway .
Mutant phenotypes:
KEGG: mfa:Mfla_1862
STRING: 265072.Mfla_1862