This entry includes tripartite ATP-independent periplasmic (TRAP) transporters which are substrate-binding protein (SBP)-dependent secondary transporters ubiquitous prokaryotes [1]. They are comprised of an SBP of the DctP or TAXI families and two in ...
This entry includes tripartite ATP-independent periplasmic (TRAP) transporters which are substrate-binding protein (SBP)-dependent secondary transporters ubiquitous prokaryotes [1]. They are comprised of an SBP of the DctP or TAXI families and two integral membrane proteins of unequal sizes that form the DctQ and DctM protein families (the small and large membrane components respectively) [1-3]. This entry represents the DctQ component and its homologues, which consists of five transmembrane segments. In SiaT, a protein involved in sialic acid uptake [4], this entry represents the N-terminal five transmembrane segments.
This entry represents the transmembrane segments from a diverse range of transporter proteins from the tripartite ATP-independent periplasmic (TRAP) transport system, in which the driving force for solute accumulation is an electrochemical ion gradie ...
This entry represents the transmembrane segments from a diverse range of transporter proteins from the tripartite ATP-independent periplasmic (TRAP) transport system, in which the driving force for solute accumulation is an electrochemical ion gradient and not ATP hydrolysis [3-5]. The first TRAP transporter to be characterised was the high-affinity C4-dicarboxylate transport (Dct) system from Rhodobacter capsulatus which consists of ESR (DctP) and small (DctQ) and large (DctM) integral membrane proteins [4]. In general, C4-dicarboxylate transport systems allow C4-dicarboxylates like succinate, fumarate, and malate to be taken up [1]. This entry also includes SiaM (involved in sialic acid uptake) [6] and YiaN (involved in the uptake of 2,3-diketo-L-gulonate) [2].
