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Database: UniProt
Entry: A0A1V3JVI6_9PAST
LinkDB: A0A1V3JVI6_9PAST
Original site: A0A1V3JVI6_9PAST 
ID   A0A1V3JVI6_9PAST        Unreviewed;       440 AA.
AC   A0A1V3JVI6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=C4-dicarboxylate transporter {ECO:0000256|PIRNR:PIRNR004539};
GN   ORFNames=BKL51_09205 {ECO:0000313|EMBL:OOF62721.1};
OS   Rodentibacter sp. Ppn85.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Rodentibacter.
OX   NCBI_TaxID=1908525 {ECO:0000313|EMBL:OOF62721.1, ECO:0000313|Proteomes:UP000189325};
RN   [1] {ECO:0000313|EMBL:OOF62721.1, ECO:0000313|Proteomes:UP000189325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ppn85 {ECO:0000313|EMBL:OOF62721.1,
RC   ECO:0000313|Proteomes:UP000189325};
RA   Christensen H.;
RT   "Rodentibacter gen. nov. and new species.";
RL   Submitted (OCT-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:OOF62721.1}.
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DR   EMBL; MLHS01000055; OOF62721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3JVI6; -.
DR   STRING; 1908525.BKL51_09205; -.
DR   OrthoDB; 9770910at2; -.
DR   Proteomes; UP000189325; 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        30..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        54..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        296..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        364..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        417..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   440 AA;  46584 MW;  AC73BE7BA22F00F6 CRC64;
     MSAMFLLQFA IVLLCILVGA RVGGIGLGVF GGLGLAILSF GFGLKPAGLP IDVMFMIMAV
     VAAAAAMQAA GGLDYMIKIA TKILRRNPKH ITFIAPAVTW LFTFLAGTGH VAYSVLPVIA
     EVSRQNGIRP ERPLSMAVIA SQFAIVASPI AAAVVAVVAY LEPQGIHLGD VLMVTVPATL
     LGIFLACIFV NKIGKELKDD PEYQRRLKDP KYADAFNSTT DTKELEISST AKISVSLFLF
     GALLVVLMGA IPSLRPVFDG KPMGMAHTIE IIMLSIGALI VLTCKPDSTE ITKGSVFHAG
     MRAVIAIFGI AWLGDTLMQA HMTEVKDMVK GLVETAPWTF ALALFVLSVL VNSQGATVAT
     LFPLGIALGI PAPVLIGVFV AVNGYFFVPN YGPIIASIDF DTTGTTKIGK YIFNHSFMLP
     GLLSMVFSVV IGLLLANVLL
//
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