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Bioenergetics and Transport |
Department of Biology, University of California at San Diego, La Jolla, CA, 92093-0116, USA1
Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2UH, UK 2
Author for correspondence: Milton H. Saier, Jr. Tel: +1 619 534 4084. Fax: +1 619 534 7108. e-mail: msaier{at}ucsd.edu
Tripartite ATP-independent periplasmic transporters (TRAP-T) represent a novel type of secondary active transporter that functions in conjunction with an extracytoplasmic solute-binding receptor. The best characterized TRAP-T family member is from Rhodobacter capsulatus and is specific for C4-dicarboxylates [Forward, J. A., Behrendt, M. C., Wyborn, N. R., Cross, R. & Kelly, D. J. (1997). J Bacteriol 179, 5482–5493]. It consists of three essential proteins, DctP, a periplasmic C4-dicarboxylate-binding receptor, and two integral membrane proteins, DctM and DctQ, which probably span the membrane 12 and 4 times, respectively. Homologues of DctM, DctP and DctQ were identified in all major bacterial subdivisions as well as in archaea. An orphan DctP homologue in the Gram-positive bacterium Bacillus subtilis may serve as a receptor for a two- component transcriptional regulatory system rather than as a constituent of a TRAP-T system. Phylogenetic data suggest that all present day TRAP-T systems probably evolved from a single ancestral transporter with minimal shuffling of constituents between systems. Homologous TRAP-T constituents exhibit decreasing degrees of sequence identity in the order DctM>DctP>DctQ. DctM appears to belong to a large superfamily of transporters, the ion transporter (IT) superfamily, one member of which can function by either protonmotive force- or ATP-dependent energization. It is proposed that IT superfamily members exhibit the unusual capacity to function in conjunction with auxiliary proteins that modify the transport process by providing (i) high-affinity solute reception, (ii) altered energy coupling and (iii) additional yet to be defined functions.
Keywords: ion transport, dicarboxylates, TRAP-T family , phylogeny, molecular evolution
Abbreviations: gb, GenBank; IT, ion transporter; p.m.f., protonmotive force; sp, SWISS-PROT; TC, transport classification; TMS, transmembrane spanning 
-helix; TRAP-T, tripartite ATP-independent periplasmic transporters
a Present address: MPI für marine Mikrobiologie, Celsiustr. 1, D-28359 Bremen, Germany.
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