DCTA_RHIME
ID DCTA_RHIME Reviewed; 441 AA.
AC P20672;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=C4-dicarboxylate transport protein;
GN Name=dctA; OrderedLocusNames=RB1523; ORFNames=SMb20611;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=2793824; DOI=10.1128/jb.171.10.5244-5253.1989;
RA Jiang J., Gu B., Albright L.M., Nixon B.T.;
RT "Conservation between coding and regulatory elements of Rhizobium meliloti
RT and Rhizobium leguminosarum dct genes.";
RL J. Bacteriol. 171:5244-5253(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RCR2011 / SU47;
RX PubMed=2551890; DOI=10.1128/jb.171.10.5551-5560.1989;
RA Engelke T., Jording D., Kapp D., Puehler A.;
RT "Identification and sequence analysis of the Rhizobium meliloti dctA gene
RT encoding the C4-dicarboxylate carrier.";
RL J. Bacteriol. 171:5551-5560(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JJ1c10;
RX PubMed=2134335; DOI=10.1094/mpmi-3-174;
RA Watson R.J.;
RT "Analysis of the C4-dicarboxylate transport genes of Rhizobium meliloti:
RT nucleotide sequence and deduced products of dctA, dctB, and dctD.";
RL Mol. Plant Microbe Interact. 3:174-181(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [6]
RP TOPOLOGY.
RX PubMed=8232193; DOI=10.1007/bf00280207;
RA Jording D., Puehler A.;
RT "The membrane topology of the Rhizobium meliloti C4-dicarboxylate permease
RT (DctA) as derived from protein fusions with Escherichia coli K12 alkaline
RT phosphatase (PhoA) and beta-galactosidase (LacZ).";
RL Mol. Gen. Genet. 241:106-114(1993).
CC -!- FUNCTION: Responsible for the transport of dicarboxylates such as
CC succinate, fumarate, and malate from the periplasm across the inner
CC membrane. This transport system plays an important role in the energy
CC supply of rhizobium-legume symbionts.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By succinate, fumarate, and malate.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000305}.
CC -!- CAUTION: The topology shown here is that reported by PubMed:8232193. It
CC contradicts that predicted by TM prediction programs and which has been
CC used in orthologous entries. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26252.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA63509.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M26531; AAA26248.1; -; Genomic_DNA.
DR EMBL; M26399; AAA26253.1; -; Genomic_DNA.
DR EMBL; M26399; AAA26252.1; ALT_INIT; Genomic_DNA.
DR EMBL; J03683; AAA63508.1; -; Genomic_DNA.
DR EMBL; J03683; AAA63509.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL591985; CAC49923.1; -; Genomic_DNA.
DR PIR; A33597; A33597.
DR PIR; C96032; C96032.
DR RefSeq; NP_438063.1; NC_003078.1.
DR RefSeq; WP_010976308.1; NC_003078.1.
DR AlphaFoldDB; P20672; -.
DR SMR; P20672; -.
DR STRING; 266834.SM_b20611; -.
DR EnsemblBacteria; CAC49923; CAC49923; SM_b20611.
DR GeneID; 25013056; -.
DR GeneID; 61601426; -.
DR KEGG; sme:SM_b20611; -.
DR PATRIC; fig|266834.11.peg.6446; -.
DR eggNOG; COG1301; Bacteria.
DR HOGENOM; CLU_019375_7_0_5; -.
DR OMA; YLYIAVI; -.
DR PRO; PR:P20672; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006835; P:dicarboxylic acid transport; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3860.10; -; 1.
DR HAMAP; MF_01300; C4_dicarb_transport; 1.
DR InterPro; IPR023954; C4_dicarb_transport.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR42865; PTHR42865; 1.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Plasmid; Reference proteome;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..441
FT /note="C4-dicarboxylate transport protein"
FT /id="PRO_0000202109"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 31..49
FT /note="Helical; Name=1"
FT TOPO_DOM 50..68
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 69..87
FT /note="Helical; Name=2"
FT TOPO_DOM 88..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 100..118
FT /note="Helical; Name=3"
FT TOPO_DOM 119..149
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 150..168
FT /note="Helical; Name=4"
FT TOPO_DOM 169..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 172..190
FT /note="Helical; Name=5"
FT TOPO_DOM 191..209
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 210..228
FT /note="Helical; Name=6"
FT TOPO_DOM 229..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 242..260
FT /note="Helical; Name=7"
FT TOPO_DOM 261..281
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 282..300
FT /note="Helical; Name=8"
FT TOPO_DOM 301..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 321..339
FT /note="Helical; Name=9"
FT TOPO_DOM 340..350
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 351..369
FT /note="Helical; Name=10"
FT TOPO_DOM 370..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 379..398
FT /note="Helical; Name=11"
FT TOPO_DOM 399..405
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
FT TRANSMEM 406..424
FT /note="Helical; Name=12"
FT TOPO_DOM 425..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8232193"
SQ SEQUENCE 441 AA; 46143 MW; B926FE7E3DC8B67D CRC64;
MIIEHSAEVR GKTPLYRHLY VQVLAAIAAG ILLGHFYPDI GTELKPLGDA FIRLVKMIIA
PVIFLTVATG IAGMTDLAKV GRVAGKAMIY FLAFSTLALV VGLVVANVVQ PGAGMHIDPA
SLDAKAVATY AEKAHEQSIT GFLMNIIPTT LVGAFAEGDI LQVLFISVLF GISLAIVGKK
AEPVVDFLQA LTLPIFRLVA ILMKAAPIGA FGAMAFTIGK YGIASIANLA MLIGTFYLTS
FLFVFIVLGA VARYNGFSIL SLIRYIKEEL LLVLGTSSSE AALPGLMNKM EKAGCKRSVV
GLVIPTGYSF NLDGTNIYMT LAALFIAQAT DTPLSYGDQI LLLLVAMLSS KGAAGITGAG
FITLAATLSV VPSVPVAGMA LILGIDRFMS ECRALTNFVG NAVATIVVAK WEGELDQAQL
SAALGGEASV EAIPAVVQPA E
