ID   DCTA_BACSU              Reviewed;         421 AA.
AC   P96603;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=C4-dicarboxylate transport protein;
DE   AltName: Full=C4-dicarboxylate permease;
GN   Name=dctA; Synonyms=dctP, ydbH; OrderedLocusNames=BSU04470;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, AND GENE NAME.
RC   STRAIN=168;
RX   PubMed=10708364; DOI=10.1099/00221287-146-2-263;
RA   Asai K., Baik S.-H., Kasahara Y., Moriya S., Ogasawara N.;
RT   "Regulation of the transport system for C4-dicarboxylic acids in Bacillus
RT   subtilis.";
RL   Microbiology 146:263-271(2000).
CC   -!- FUNCTION: Responsible for the transport of succinate and fumarate, but
CC       not malate, across the membrane. {ECO:0000305|PubMed:10708364}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Induced by succinate and fumarate. Expression of dctA
CC       requires the DctB, DctS and DctR proteins and is decreased in the
CC       presence of malate.
CC   -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC       (DAACS) (TC 2.A.23) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB001488; BAA19284.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12254.1; -; Genomic_DNA.
DR   PIR; C69771; C69771.
DR   RefSeq; NP_388328.1; NC_000964.3.
DR   RefSeq; WP_003246626.1; NZ_JNCM01000031.1.
DR   AlphaFoldDB; P96603; -.
DR   SMR; P96603; -.
DR   STRING; 224308.BSU04470; -.
DR   TCDB; 2.A.23.1.6; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR   PaxDb; P96603; -.
DR   PRIDE; P96603; -.
DR   EnsemblBacteria; CAB12254; CAB12254; BSU_04470.
DR   GeneID; 938223; -.
DR   KEGG; bsu:BSU04470; -.
DR   PATRIC; fig|224308.179.peg.473; -.
DR   eggNOG; COG1301; Bacteria.
DR   InParanoid; P96603; -.
DR   OMA; QATNTPM; -.
DR   PhylomeDB; P96603; -.
DR   BioCyc; BSUB:BSU04470-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015138; F:fumarate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015366; F:malate:proton symporter activity; IBA:GO_Central.
DR   GO; GO:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0070778; P:L-aspartate transmembrane transport; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..421
FT                   /note="C4-dicarboxylate transport protein"
FT                   /id="PRO_0000202090"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   421 AA;  45441 MW;  29FA5A6BD5DD7A5A CRC64;
     MKLFKNLTVQ VITAVIIGVI VGLVWPDVGK EMKPLGDTFI NAVKMVIAPI IFFTIVLGIA
     KMGDMKKVGK VGGKAFIYFE VVTTLALIIG LFVVNIMKPG AGLDYSKLEK GDVSQYTQNG
     GQGIDWIEFI THIVPSNMVD AFAKGDILQV LFFSILFGVG LAALGEKGKS VIDFFDKVSH
     VFFKIIGYIM RAAPIGAFGA MAYTIGHFGL DSIKPLASLM MSVYITMFLF VFVALNIICK
     LYGFSLWNYL RFIKDELLIV LGTSSSESVL PRMMDKMERY GCSKSVVGLV IPTGYSFNLD
     GTSIYLSMAT VFLAQVFGVD LSIGQQITII LVLMLTSKGA AGVTGSGFIV LASTLSALQV
     IPLEGLALLL GVDRFMSEGR AIVNLIGNGI ATIIVAKSEN EFDEAKSIEA VEGMKKMKTA
     V