| Primary Identifier | IPR028611 | Type | Family |
| Short Name | DmsD_chaperone |
| description | DmsD is essential for the biogenesis/assembly of dimethyl sulfoxide (DMSO) reductase in Escherichia coli. DmsD binds the signal peptide of DmsA - the catalytic subunit of the DMSO reductase and a substrate for the Twin-arginine translocase (Tat) pathway - but it is not required for the interaction of the DmsA signal peptide with the Tat system [, ]. DmsD may be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein []. |
