Disulfide oxidoreductase D
family of transport proteins
The Disulfide bond oxidoreductase D (DsbD) family is a member of the Lysine Exporter (LysE) Superfamily. A representative list of proteins belonging to the DsbD family can be found in the Transporter Classification Base.
Homology
Homologues include:
(1) several thiol-disulfide exchange proteins (i.e., TC# 5.A.1.1.1)
(2) the cytochrome c-type biogenesis proteins, CcdA (TC# 5.A.1.2.1) of Paracoccus pantotrophus and Bacillus subtilis.
(3) the methylamine utilization proteins, MauF (TC# 5.A.1.3.1) of Paracoccus denitrificans and P. versutus.
(4) the mercury resistance proteins (TC# 5.A.1.4.1; possibly Hg2+ transporters) of Mycobacterium tuberculosis and Streptomyces lividans.
(5) suppressors of copper sensitivity (TC# 5.A.1.5.1; copper tolerance proteins) of Salmonella typhimurium and Vibrio cholerae.
(6) components of peroxide reduction pathways (TC# 5.A.1.5.2), and
(7) components of sulfenic acid reductases.
Disulfide bond oxidoreductase D (DsbD)
The best characterized member of the DsbD family is DsbD of E. coli (TC# 5.A.1.1.1). The DsbD protein is membrane-embedded with a putative N-terminal transmembrane segment (TMS) plus 8 additionalTMSs. The smallest homologues (190 aas with 6 putative TMSs) are found in archaea, while the largest are found in both Gram-negative bacteria (758 aas with 9 putative TMSs) and Gram-positive bacteria (695 aas with 6 putative TMSs).
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