v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes [ , , ]. This protein family includes the bacilliredoxins BrxA and BrxB (previously known as YphP and YqiW, respectively) and uncharacterised proteins from bacteria. BrxA and BrxB debacillithiolate (remove BSH) the S-bacillithiolated OhrR (OhrR-SSB) and in vivo NaOCl-generated S-bacillithiolated MetE (MetE-SSB). Both proteins are involved in maintaining redox homeostasis in response to disulfide stress conditions [ ]. The crystal structure of BrxA shows similarity with a thioredoxin fold. It has a CXC motif that plays a key role in catalytic activity []. |
| Short Name | BrxB/BrxA |