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DCTP_RHOCA
ID   DCTP_RHOCA              Reviewed;         333 AA.
AC   P37735;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=C4-dicarboxylate-binding periplasmic protein DctP {ECO:0000305};
DE   Flags: Precursor;
GN   Name=dctP {ECO:0000303|PubMed:1809844};
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-43, AND FUNCTION.
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=1809844; DOI=10.1111/j.1365-2958.1991.tb01865.x;
RA   Shaw J.G., Hamblin M.J., Kelly D.J.;
RT   "Purification, characterization and nucleotide sequence of the periplasmic
RT   C4-dicarboxylate-binding protein (DctP) from Rhodobacter capsulatus.";
RL   Mol. Microbiol. 5:3055-3062(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE,
RP   AND NOMENCLATURE.
RX   PubMed=9287004; DOI=10.1128/jb.179.17.5482-5493.1997;
RA   Forward J.A., Behrendt M.C., Wyborn N.R., Cross R., Kelly D.J.;
RT   "TRAP transporters: a new family of periplasmic solute transport systems
RT   encoded by the dctPQM genes of Rhodobacter capsulatus and by homologs in
RT   diverse gram-negative bacteria.";
RL   J. Bacteriol. 179:5482-5493(1997).
RN   [3]
RP   FUNCTION, SUBSTRATE-BINDING, AND SUBCELLULAR LOCATION.
RX   PubMed=1569065; DOI=10.1016/s0021-9258(18)42408-8;
RA   Walmsley A.R., Shaw J.G., Kelly D.J.;
RT   "The mechanism of ligand binding to the periplasmic C4-dicarboxylate
RT   binding protein (DctP) from Rhodobacter capsulatus.";
RL   J. Biol. Chem. 267:8064-8072(1992).
CC   -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC       transport system DctPQM involved in C4-dicarboxylates uptake. Binds C4-
CC       dicarboxylates such as fumarate, succinate, L-malate and D-malate.
CC       {ECO:0000269|PubMed:1569065, ECO:0000269|PubMed:1809844,
CC       ECO:0000269|PubMed:9287004}.
CC   -!- SUBUNIT: The complex comprises the extracytoplasmic solute receptor
CC       protein DctP, and the two transmembrane proteins DctQ and DctM.
CC       {ECO:0000269|PubMed:9287004}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1569065}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant is unable to transport succinate,
CC       and does not grow on D-malate, L-malate, succinate or fumarate as the
CC       sole carbon source under aerobic conditions in the dark.
CC       {ECO:0000269|PubMed:9287004}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC       {ECO:0000305}.
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DR   EMBL; X63974; CAA45385.1; -; Genomic_DNA.
DR   PIR; S18578; S18578.
DR   AlphaFoldDB; P37735; -.
DR   SMR; P37735; -.
DR   TCDB; 2.A.56.1.1; the tripartite atp-independent periplasmic transporter (trap-t) family.
DR   GeneID; 31491816; -.
DR   OMA; FRIMPSE; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 3.40.190.170; -; 1.
DR   InterPro; IPR018389; DctP_fam.
DR   InterPro; IPR004682; TRAP_DctP.
DR   InterPro; IPR038404; TRAP_DctP_sf.
DR   PANTHER; PTHR33376; PTHR33376; 1.
DR   Pfam; PF03480; DctP; 1.
DR   PIRSF; PIRSF006470; DctB; 1.
DR   TIGRFAMs; TIGR00787; dctP; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Periplasm; Signal; Sugar transport; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:1809844"
FT   CHAIN           27..333
FT                   /note="C4-dicarboxylate-binding periplasmic protein DctP"
FT                   /id="PRO_0000031812"
SQ   SEQUENCE   333 AA;  36128 MW;  246628AEC0752381 CRC64;
     MLTRRILGAL VGATALSLAL SVPALAEPIV IKFSHVVAPD TPKGKGAAKF EELAEKYTNG
     AVDVEVYPNS QLYKDKEELE ALQLGAVQML APSLAKFGPL GVQDFEVFDL PYIFKDYEAL
     HKVTQGEAGK MLLSKLEAKG ITGLAFWDNG FKIMSANTPL TMPDDFLGLK MRIQSSKVLE
     AEMNALGAVP QVMAFSEVYQ ALQTGVVDGT ENPPSNMFTQ KMNEVQKHAT VSNHGYLGYA
     VIVNKQFWDG LPADVRTGLE KAMAESTDYA NGIAKEENEK ALQAMKDAGT TEFHELTAEE
     RAAWEEVLTP VHDEMAERIG AETIAAVKAA TAE
 
 
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