dsbB
dsbB encodes DsbB, a membrane-anchored oxidoreductase that participates in disulfide bond formation in the periplasm of many Gram-negative bacteria. It works in the bacterial Dsb (disulfide bond) system to ensure proper folding of extracytoplasmic proteins, many of which require disulfide bonds for stability and activity. DsbA is the primary oxidase that introduces disulfide bonds into substrate proteins, becoming reduced in the process; DsbB reoxidizes DsbA, transferring electrons from DsbA to the membrane quinone pool and thereby sustaining continuous disulfide bond formation.
Mechanism-wise, DsbB is an inner membrane protein with multiple transmembrane helices. It contains conserved cysteine residues
Genetically, dsbB is part of the broader dsb oxidative pathway and is commonly found in conjunction with
Distribution and significance, in short,: the dsbA–dsbB pair is widely conserved among Gram-negative bacteria and is