ID   DCTA_SHIFL              Reviewed;         428 AA.
AC   Q83PS4; Q7BYY4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=C4-dicarboxylate transport protein {ECO:0000255|HAMAP-Rule:MF_01300};
GN   Name=dctA {ECO:0000255|HAMAP-Rule:MF_01300};
GN   OrderedLocusNames=SF3560, S4207;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Responsible for the transport of dicarboxylates such as
CC       succinate, fumarate, and malate from the periplasm across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01300}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01300}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01300}.
CC   -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC       (DAACS) (TC 2.A.23) family. {ECO:0000255|HAMAP-Rule:MF_01300}.
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; AE005674; AAN45013.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP19172.1; -; Genomic_DNA.
DR   RefSeq; NP_709306.1; NC_004337.2.
DR   RefSeq; WP_000858217.1; NZ_WPGW01000020.1.
DR   AlphaFoldDB; Q83PS4; -.
DR   SMR; Q83PS4; -.
DR   STRING; 198214.SF3560; -.
DR   EnsemblBacteria; AAN45013; AAN45013; SF3560.
DR   EnsemblBacteria; AAP19172; AAP19172; S4207.
DR   GeneID; 1026337; -.
DR   KEGG; sfl:SF3560; -.
DR   KEGG; sft:NCTC1_03842; -.
DR   KEGG; sfx:S4207; -.
DR   PATRIC; fig|198214.7.peg.4194; -.
DR   HOGENOM; CLU_019375_7_0_6; -.
DR   OMA; YLYIAVI; -.
DR   OrthoDB; 781228at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..428
FT                   /note="C4-dicarboxylate transport protein"
FT                   /id="PRO_1000067468"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        184..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
SQ   SEQUENCE   428 AA;  45402 MW;  568FDC54F1AA7EB8 CRC64;
     MKTSLFKSLY FQVLTAIAIG ILLGHFYPEI GEQMKPLGDG FVKLIKMIIA PVIFCTVVTG
     IAGMESMKAV GRTGAVALLY FEIVSTIALI IGLIIVNVVQ PGAGMNVDPA TLDAKAVAVY
     ADQAKDQGIV AFIMDVIPAS VIGAFASGNI LQVLLFAVLF GFALHRLGSK GQLIFNVIES
     FSQVIFGIIN MIMRLAPIGA LGAMAFTIGK YGVGTLVQLG QLIICFYITC ILFVVLVLGS
     IAKATGFSIF KFIRYIREEL LIVLGTSSSE SALPRMLDKM EKLGCRKSVV GLVIPTGYSF
     NLDGTSIYLT MAAVFIAQAT NSQMDIVHQI TLLIVLLLSS KGAAGVTGSG FIVLAATLSA
     VGHLPVAGLA LILGIDRFMS EARALTNLVG NGVATIVVAK WVKELDHKKL DDVLNNRAPD
     GKTHELSS