v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | The tripartite ATP-independent periplasmic (TRAP) transporters are substrate-binding protein (SBP)-dependent secondary transporters found in prokaryotes. They consist of a substrate-binding protein (SBP) of the DctP or TAXI families and two integral membrane proteins that form the DctQ and DctM protein families [ ].This entry represents the DctP family of the substrate-binding proteins. They are part of the DctP-TRAP (tripartite ATP-independent periplasmic) transporter involved in binding extracellular solutes for transport across the bacterial cytoplasmic membrane. Proteins in this family include DctP from R. capsulatus, SiaP from Haemophilus influenzae [], DctB from Bacillus subtilis [], and TeaA from Halomonas elongata []. The structure of the SiaP receptor has revealed an overall topology similar to ATP binding cassette ESR (extracytoplasmic solute receptors) proteins []. Upon binding of sialic acid, SiaP undergoes domain closure about a hinge region and kinking of an α-helix hinge component []. |
| Short Name | DctP_fam |