DCTQ_RHOCA
ID DCTQ_RHOCA Reviewed; 227 AA.
AC O07837;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=C4-dicarboxylate TRAP transporter small permease protein DctQ {ECO:0000305};
GN Name=dctQ {ECO:0000303|PubMed:9287004};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND NOMENCLATURE.
RC STRAIN=ATCC 33303 / B10;
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 [2]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11150659; DOI=10.1111/j.1574-6968.2001.tb09439.x;
RA Wyborn N.R., Alderson J., Andrews S.C., Kelly D.J.;
RT "Topological analysis of DctQ, the small integral membrane protein of the
RT C4-dicarboxylate TRAP transporter of Rhodobacter capsulatus.";
RL FEMS Microbiol. Lett. 194:13-17(2001).
CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system DctPQM involved in C4-dicarboxylates uptake.
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: Cell inner membrane {ECO:0000269|PubMed:11150659,
CC ECO:0000269|PubMed:9287004}; Multi-pass membrane protein {ECO:0000255}.
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 TRAP transporter small permease family.
CC {ECO:0000305}.
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DR EMBL; X63974; CAA45386.1; -; Genomic_DNA.
DR RefSeq; WP_013068720.1; NZ_VIBE01000005.1.
DR AlphaFoldDB; O07837; -.
DR TCDB; 2.A.56.1.1; the tripartite atp-independent periplasmic transporter (trap-t) family.
DR GeneID; 31491815; -.
DR OMA; LEWPTWI; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR007387; TRAP_DctQ.
DR PANTHER; PTHR35011; PTHR35011; 1.
DR Pfam; PF04290; DctQ; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..227
FT /note="C4-dicarboxylate TRAP transporter small permease
FT protein DctQ"
FT /id="PRO_0000435382"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11150659"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..67
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11150659"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11150659"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..149
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11150659"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11150659"
SQ SEQUENCE 227 AA; 24763 MW; 0DE9D59DE5450F99 CRC64;
MLRILDRAEE VLIAALIATA TVLIFVSVTH RFTLGFVADF VGFFRGHGMT GAAAAAKSLY
TTLRGINLVW AQELCIILFV WMAKFGAAYG VRTGIHVGID VLINRLDAPK RRFFILLGLG
AGALFTGIIA TLGANFVLHM YHASSTSPDL ELPMWLVYLA IPMGSSLMCF RFLQVAFGFA
RTGELPHHDH GHVDGVDTEN EGIDAEGDVL LHSPLTPRDL VEKPKDN