Protein Family Models

This family of proteins has disulphide isomerase activity, EC:5.3.4.1. It has a similar fold to thioredoxin, with an alpha-beta-alpha-beta-alpha-beta-beta-alpha topology. It has a conserved CGC motif in the loop immediately downstream of the first beta strand. This motif is essential for activity [1]. [1]. 19653655. Structure and function of Bacillus subtilis YphP, a prokaryotic. disulfide isomerase with a CXC catalytic motif .. Derewenda U, Boczek T, Gorres KL, Yu M, Hung LW, Cooper D,. Joachimiak A, Raines RT, Derewenda ZS;. Biochemistry. 2009;48:8664-8671. (from Pfam)

Date:

2024-08-14

Gene:

brxB

Date:

2023-06-30

BrxA/BrxB family bacilliredoxin which may catalyze the removal of bacillithiol that becomes linked to protein thiols under oxidative stress; may participate in a complex catalyzing the removal of S-thioallylations from proteins caused by allicin stress

Date:

2019-08-12

This protein family is one of several observed in species that express bacillithiol, an analog of glutathione and mycothiol. Rather than being involved in bacillithiol biosynthesis, members are likely to act in bacillithiol-dependent processes. A suggested term is bacilliredoxin (a glutaredoxin-like thiol-dependent oxidoreductase), and a suggested role of YphP is de-bacillithiolation - removing bacillithiol that became linked to protein thiols under oxidative stress. An older description of YphP as a disulphide isomerase therefore may be wrong.

Date:

2019-09-10