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Database: UniProt
Entry: C5S4E7_9PAST
LinkDB: C5S4E7_9PAST
Original site: C5S4E7_9PAST 
ID   C5S4E7_9PAST            Unreviewed;       440 AA.
AC   C5S4E7;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=C4-dicarboxylate transporter {ECO:0000256|PIRNR:PIRNR004539};
GN   ORFNames=AM305_02663 {ECO:0000313|EMBL:EER46218.1};
OS   Actinobacillus minor NM305.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=637911 {ECO:0000313|EMBL:EER46218.1, ECO:0000313|Proteomes:UP000005532};
RN   [1] {ECO:0000313|EMBL:EER46218.1, ECO:0000313|Proteomes:UP000005532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NM305 {ECO:0000313|EMBL:EER46218.1,
RC   ECO:0000313|Proteomes:UP000005532};
RX   PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA   Arya G., Niven D.F.;
RT   "Production of haemolysins by strains of the Actinobacillus
RT   minor/"porcitonsillarum" complex.";
RL   Vet. Microbiol. 141:332-341(2010).
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:EER46218.1}.
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DR   EMBL; ACQL01000135; EER46218.1; -; Genomic_DNA.
DR   RefSeq; WP_005825681.1; NZ_ACQL01000135.1.
DR   AlphaFoldDB; C5S4E7; -.
DR   eggNOG; COG2704; Bacteria.
DR   OrthoDB; 9770910at2; -.
DR   Proteomes; UP000005532; 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        6..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        134..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        235..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        266..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;  46536 MW;  85A5A8C512A673B9 CRC64;
     MSAMFILQFA IVLLCILIGA RVGGIGLGVF GGLGLAILSF GFGLKPAGLP IDVMFMIMAV
     VSAAAAMQAA GGLDYMIKIA TNILRRNPKY ITFIAPLVTW TFTVLAGTGH VAYSVLPVIA
     EVSRHNGVRP ERPLSMAVIA SQFAIVASPI AAAVVAVVAF LEPQGITLGD VLMVTIPSTL
     LGLMLACVFV NKMGKELKDD PHYQKLLQDP EYVKANHTDT NPAEVVIKPT AKMSVGLFLF
     GALLVVLLGA MPSLRPVFDG KPMGMAHAIE IVMLTVGALI ILFCKPDGDE ITKGSIFHAG
     MRAVIAIFGI AWLGDTLMQA HMTEVKEMVS GLVEAAPWAF ALALFVLSIL VNSQGATVAT
     LFPLAVAIGI PAPILIGVFV AVNGYFFIPN YGPIIASIDF DTTGTTRIGK FIFNHSFMLP
     GLISMAFCLG LGLLFAQIFL
//
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