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Database: UniProt
Entry: A0A1A9S1D1_9NEIS
LinkDB: A0A1A9S1D1_9NEIS
Original site: A0A1A9S1D1_9NEIS 
ID   A0A1A9S1D1_9NEIS        Unreviewed;       439 AA.
AC   A0A1A9S1D1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=C4-dicarboxylate transporter {ECO:0000256|PIRNR:PIRNR004539};
GN   ORFNames=A7P95_02530 {ECO:0000313|EMBL:OAM30913.1};
OS   Eikenella longinqua.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Eikenella.
OX   NCBI_TaxID=1795827 {ECO:0000313|EMBL:OAM30913.1, ECO:0000313|Proteomes:UP000077885};
RN   [1] {ECO:0000313|Proteomes:UP000077885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML02-A-017 {ECO:0000313|Proteomes:UP000077885};
RA   Bernier A.-M., Bernard K.;
RT   "Draft genome of Corynebacterium afermentans subsp. afermentans LCDC
RT   88199T.";
RL   Submitted (MAY-2016) 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) + 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAM30913.1}.
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DR   EMBL; LXSL01000012; OAM30913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A9S1D1; -.
DR   STRING; 1795827.A7P95_02530; -.
DR   OrthoDB; 9770910at2; -.
DR   Proteomes; UP000077885; Unassembled WGS sequence.
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:SF1; 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   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        7..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        231..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        333..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        362..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        415..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   439 AA;  46231 MW;  E7E0EB4CC3574A3F CRC64;
     MQFFIQFAVV LLCILAGARV GGIGLGVFGG VGLAVLSFGF GLEPTSPPID VMLMIMAVVS
     AAAAMQAAGG LDYMIKIATR VLHKNPKYIT FIAPMVTYSF TVLAGTGHVA YSVLPVIAEV
     SRKNGIRPER PLSMAVIASQ FAIIASPIAA AVVACVSYLE PQHITMADVL KVSIPSTVLG
     IGIACVLVNK MGKELKDDPE YQRRPQDPAY RKLYEAETAV ADTEVGAKAK ISVGIFLFAA
     ILVVLLGALP SLRPVFNDKP MGMAHTIEIV MLAAAALIIV TCKPDGNAIT QGSVFHAGMR
     AVIAVFGVAW LGDTLMHGHL DEVKMAVSGL VESAPWAFTF ALFVLSVLVN SQGATVATLF
     PVAIALGVSA PIIIGTFVAV NGYFFIPNYG PIIAAIDFDS TGTTKIGKYI FNHSFMLPGL
     LSMGFSLVLG LMFAKMFLG
//
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