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Database: UniProt
Entry: W0HIW1_9GAMM
LinkDB: W0HIW1_9GAMM
Original site: W0HIW1_9GAMM 
ID   W0HIW1_9GAMM            Unreviewed;       444 AA.
AC   W0HIW1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=C4-dicarboxylate transporter {ECO:0000256|PIRNR:PIRNR004539};
GN   ORFNames=SOPEG_1537 {ECO:0000313|EMBL:AHF73699.1};
OS   Candidatus Sodalis pierantonius str. SOPE.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=2342 {ECO:0000313|EMBL:AHF73699.1, ECO:0000313|Proteomes:UP000019025};
RN   [1] {ECO:0000313|EMBL:AHF73699.1, ECO:0000313|Proteomes:UP000019025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=none {ECO:0000313|Proteomes:UP000019025};
RX   PubMed=24407854; DOI=10.1093/gbe/evt210;
RA   Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA   Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA   Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT   "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL   Genome Biol. Evol. 6:76-93(2014).
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) + 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}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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; CP006568; AHF73699.1; -; Genomic_DNA.
DR   RefSeq; WP_025244972.1; NZ_CP006568.1.
DR   AlphaFoldDB; W0HIW1; -.
DR   STRING; 2342.SOPEG_1537; -.
DR   KEGG; pes:SOPEG_1537; -.
DR   PATRIC; fig|2342.5.peg.1635; -.
DR   eggNOG; COG2704; Bacteria.
DR   HOGENOM; CLU_036056_1_1_6; -.
DR   Proteomes; UP000019025; 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   PANTHER; PTHR36106; ANAEROBIC C4-DICARBOXYLATE TRANSPORTER DCUB; 1.
DR   PANTHER; PTHR36106:SF3; ANAEROBIC C4-DICARBOXYLATE TRANSPORTER DCUB; 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|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:UP000019025};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR004539}.
FT   TRANSMEM        52..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        234..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        419..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   444 AA;  46663 MW;  11791B3D0A03D133 CRC64;
     MEFIIQLTVV VVCLLFGARK GGIGLGLAGG CGMLTLVWIF DLQPGQPPVD VMLVIIAVVA
     ASATLQASGG LDVLLQLAEK LLRRNPKYIS LVAPLVTCLL TMLCGTGHVV YTLLPIIYDV
     AIKNNIRPER PLAASSIGSQ MGIIASPVSV ATVSLAAMLA LSGSAAIDFI TLLSLTIPAT
     LCGILAIALF SGFRGKDLRD DDDFLAFINT KDNHDYVYGT APTLLNSTLP RSSWLAMGIF
     IATILVIALL GAFPALRPHG NGVPLSMVLM IQMCMLCGGA FIVLFTDTAL AAITKNDVFR
     SGMVAIVAVY GVAWMADTLF SHHLLQIEAA LAGVVSDHPW TYALALLLLS QFVNSQAAAL
     AAVVPIALAV GVPPALIAAT APTCYGYYIL PTYPSDLAAV QFDRAGTTRI GRWVINHSFL
     PVGLIGVGVS CCVGWLLAHA YGLM
//
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