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}.
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; 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
//