ID DCTA_LEPCP Reviewed; 447 AA.
AC B1Y0B2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=C4-dicarboxylate transport protein {ECO:0000255|HAMAP-Rule:MF_01300};
GN Name=dctA {ECO:0000255|HAMAP-Rule:MF_01300}; OrderedLocusNames=Lcho_4340;
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for the transport of dicarboxylates such as
CC succinate, fumarate, and malate from the periplasm across the membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01300}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01300}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01300}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000255|HAMAP-Rule:MF_01300}.
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DR EMBL; CP001013; ACB36591.1; -; Genomic_DNA.
DR RefSeq; WP_012349332.1; NC_010524.1.
DR AlphaFoldDB; B1Y0B2; -.
DR SMR; B1Y0B2; -.
DR STRING; 395495.Lcho_4340; -.
DR KEGG; lch:Lcho_4340; -.
DR eggNOG; COG1301; Bacteria.
DR HOGENOM; CLU_019375_7_0_4; -.
DR OrthoDB; 9766690at2; -.
DR Proteomes; UP000001693; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006835; P:dicarboxylic acid transport; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3860.10; Sodium:dicarboxylate symporter; 1.
DR HAMAP; MF_01300; C4_dicarb_transport; 1.
DR InterPro; IPR023954; C4_dicarb_transport.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR42865:SF1; AEROBIC C4-DICARBOXYLATE TRANSPORT PROTEIN; 1.
DR PANTHER; PTHR42865; PROTON/GLUTAMATE-ASPARTATE SYMPORTER; 1.
DR Pfam; PF00375; SDF; 1.
DR PRINTS; PR00173; EDTRNSPORT.
DR SUPFAM; SSF118215; Proton glutamate symport protein; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..447
FT /note="C4-dicarboxylate transport protein"
FT /id="PRO_1000140460"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT REGION 422..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 47616 MW; 716C61A38411B784 CRC64;
MHTPSGPLPF YRSLYFQVIT AIVIGVLLGH YWPETGTAMK PLGDGFIKLI KMIIAPIIFC
TVVVGIAGME DMKRVGKTGG LALLYFEVVS TLALLLGLLI VNLVQPGVGM HVDPATLDTK
GIAAYTAPGK MQTTTEFLLA VIPTTVVDAF AKGEMLQVLL FSVMFGFALH QFGGRGTLVF
DFIEKTSHVL FAIVGFIMKV APIGAFGAMA FTIGKYGLGS LIPLAKLMGT FYATCLVFIF
GVLGLIAKAH GFSIWKFIKY IKEELLIVLG TSSSESVLPR MMAKLENLGV RKSTVGLVVP
TGYSFNLDGT SIYLTMAAVF IAQATDTPMT LTQQLTLLAV LLLTSKGAAG VTGSGFIVLA
ATLSAVGGVP VAGLALILGI DRFMSEARAL TNLIGNGVAT VVVGKWTGDL DEKQMRYHLD
RETEAEANEP EAVLDEIDQH MPVPAAR
//
