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Database: UniProt
Entry: A0A0A7A3L9_SHIDY
LinkDB: A0A0A7A3L9_SHIDY
Original site: A0A0A7A3L9_SHIDY 
ID   A0A0A7A3L9_SHIDY        Unreviewed;       433 AA.
AC   A0A0A7A3L9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   18-JUN-2025, entry version 40.
DE   RecName: Full=C4-dicarboxylate transporter {ECO:0000256|PIRNR:PIRNR004539};
GN   ORFNames=Asd1617_05827 {ECO:0000313|EMBL:AHA68654.1};
OS   Shigella dysenteriae 1617.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=754093 {ECO:0000313|EMBL:AHA68654.1, ECO:0000313|Proteomes:UP000031647};
RN   [1] {ECO:0000313|EMBL:AHA68654.1, ECO:0000313|Proteomes:UP000031647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1617 {ECO:0000313|EMBL:AHA68654.1,
RC   ECO:0000313|Proteomes:UP000031647};
RA   Aksomboon Vongsawan A., Kapatral V., Vaisvil B., Serichantalergs O.,
RA   Hale T.L., Mason C.J.;
RT   "Comparative genomics of Sd1617 to representative strains in evaluating its
RT   pathogenesis.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Responsible for the transport of C4-dicarboxylates.
CC       {ECO:0000256|PIRNR:PIRNR004539}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate(in) + succinate(out) = (S)-malate(out) +
CC         succinate(in); Xref=Rhea:RHEA:29327, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:30031; Evidence={ECO:0000256|ARBA:ARBA00034284};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29329;
CC         Evidence={ECO:0000256|ARBA:ARBA00034284};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate(in) + succinate(out) = L-aspartate(out) +
CC         succinate(in); Xref=Rhea:RHEA:29343, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:30031; Evidence={ECO:0000256|ARBA:ARBA00034237};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29345;
CC         Evidence={ECO:0000256|ARBA:ARBA00034237};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=fumarate(in) + L-aspartate(out) = fumarate(out) + L-
CC         aspartate(in); Xref=Rhea:RHEA:72459, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:29991; Evidence={ECO:0000256|ARBA:ARBA00036117};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72460;
CC         Evidence={ECO:0000256|ARBA:ARBA00036117};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=fumarate(in) + succinate(out) = fumarate(out) + succinate(in);
CC         Xref=Rhea:RHEA:29323, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031;
CC         Evidence={ECO:0000256|ARBA:ARBA00034287};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29325;
CC         Evidence={ECO:0000256|ARBA:ARBA00034287};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|PIRNR:PIRNR004539}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC       ECO:0000256|PIRNR:PIRNR004539}.
CC   -!- SIMILARITY: Belongs to the DcuA/DcuB transporter (TC 2.A.13.1) family.
CC       {ECO:0000256|ARBA:ARBA00006413, ECO:0000256|PIRNR:PIRNR004539}.
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DR   EMBL; CP006736; AHA68654.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A7A3L9; -.
DR   KEGG; sdz:Asd1617_05827; -.
DR   PATRIC; fig|754093.4.peg.5694; -.
DR   HOGENOM; CLU_036056_1_1_6; -.
DR   Proteomes; UP000031647; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015556; F:C4-dicarboxylate transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR004668; Anaer_Dcu_memb_transpt.
DR   NCBIfam; TIGR00770; Dcu; 1.
DR   NCBIfam; NF006927; PRK09412.1; 1.
DR   NCBIfam; NF009136; PRK12489.1; 1.
DR   PANTHER; PTHR36106; ANAEROBIC C4-DICARBOXYLATE TRANSPORTER DCUB; 1.
DR   PANTHER; PTHR36106:SF2; C4-DICARBOXYLATE TRANSPORTER DCUA; 1.
DR   Pfam; PF03605; DcuA_DcuB; 1.
DR   PIRSF; PIRSF004539; C4-dicrbxl_trns; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW   ECO:0000256|PIRNR:PIRNR004539};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR004539};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR004539};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031647};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR004539}.
FT   TRANSMEM        6..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        289..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        357..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        410..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   433 AA;  45708 MW;  2109B44BF9BD05BE CRC64;
     MLVVELIIVL LAIFLGARLG GIGIGFAGGL GVLVLAAIGV KPGNIPFDVI SIIMAVIAAI
     SAMQVAGGLD YLVHQTEKLL RRNPKYITIL APIVTYFLTI FAGTGNISLA TLPVIAEVAK
     EQGVKPCRPL STAVVSAQIA ITASPISAAV VYMSSVMEGH GISYLHLLSV VIPSTLLAVL
     VMSFLVTMLF NSKLSDDPIY RKRLEEGLVE LLGEKQIEIK SGAKTSVWLF LLGVVGVVIY
     AIINSPSMGL VEKPLMNTTN AILIIMLSVA TLTTVICKVD TDNILNSSTF KAGMSACICI
     LGVAWLGDTF VSNNIDWIKD TAGEVIQGHP WLLAVIFFFA SALLYSQAAT AKALMPMALA
     LNVSPLTAVA SFAAVSGLFI LPTYPTLVAA VQMDDTGTTR IGKFVFNHPF FIPGTLGVAL
     AVCFGFVLGS FML
//
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