| Primary Identifier | IPR020945 | Type | Family |
| Short Name | DMSO/NO3_reduct_chaperone |
| description | This entry represents a family of proteins which are involved in enzymes assembly and/or maturation: The TorD protein is involved in the maturation of the the trimethylamine N-oxide reductase TorA (a DMSO reductase family member) in Escherichia coli []. TorA is a molybdenum-containing enzyme which requires the the insertion of a bis(molybdopterin guanine dinucleotide) molybdenum (bis(MGD)Mo) cofactor in its catalytic site to be active and translocated to the periplasm. TorD acts as a chaperone, binding to apoTorA and promoting efficient incorporation of the cofactor into the protein.Nitrate reductase delta subunit (NarJ). This subunit is not part of the nitrate reductase enzyme but is a chaperone required for proper molybdenum cofactor insertion and final assembly of the nitrate reductase [, , ]. NarJ exhibits sequence homology to chaperones involved in maturation and cofactor insertion of E. coli redox enzymes that are mediated by twin-arginine translocase (Tat) dependent translocation []. The archetypal Tat proofreading chaperones belong to the TorD family [].Twin-arginine leader-binding protein DmsD, which could be required for the biogenesis of DMSO reductase rather than for the targeting of DmsA to the inner membrane [, , ].Dimethyl sulphide dehydrogenase protein DdhD. This protein is thought to function as chaperone protein in the assembly of an active dimethyl sulphide dehydrogenase DdhABC []. |
