DCTA_DEIGD
ID DCTA_DEIGD Reviewed; 442 AA.
AC Q1J1H5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=C4-dicarboxylate transport protein {ECO:0000255|HAMAP-Rule:MF_01300};
GN Name=dctA {ECO:0000255|HAMAP-Rule:MF_01300}; OrderedLocusNames=Dgeo_0356;
OS Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=319795;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11300 / AG-3a;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for the transport of dicarboxylates such as
CC succinate, fumarate, and malate across the membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01300}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01300};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-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; CP000359; ABF44659.1; -; Genomic_DNA.
DR RefSeq; WP_011529503.1; NC_008025.1.
DR AlphaFoldDB; Q1J1H5; -.
DR SMR; Q1J1H5; -.
DR STRING; 319795.Dgeo_0356; -.
DR TCDB; 2.A.23.1.9; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR EnsemblBacteria; ABF44659; ABF44659; Dgeo_0356.
DR KEGG; dge:Dgeo_0356; -.
DR eggNOG; COG1301; Bacteria.
DR HOGENOM; CLU_019375_7_0_0; -.
DR OMA; YFCTTII; -.
DR OrthoDB; 781228at2; -.
DR Proteomes; UP000002431; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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; PTHR42865; 1.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..442
FT /note="C4-dicarboxylate transport protein"
FT /id="PRO_1000067443"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 77..97
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 185..205
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT REGION 420..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 46367 MW; 7E3941CACDFBF0B9 CRC64;
MPKIFRSLYV QVLIAIVLGI LVGFLFPSFG EGLKPLGDGF IKLIKMLIAP IIFATVVSGI
AHMRDTKKVG RVGGKALIYF EVVTTFALVI GLVVANILKP GHGMNVNPAT LDTSAISKYT
QAAGEQSVAD FLLHIIPNTL VSAFTEGDLL QVLLISVLFG FALTQLGTLG QKVLAGIEAV
NSAVFVILGF VMRLAPIGAF GAMAFTIGKY GVGTLAQLAY LMVAFYATCL LFVFVVLGLI
ARFAGFSILK FIRFIKEELL LVLGTSSSES ALPRLITKLE YAGANRSVVG LVVPAGYSFN
LDGTSIYLTM ATLFIAQATN THLSLGQQLG ILGVLLLTSK GAAGVTGSGF ITLAATLSAV
GHVPVAGLAL ILGIDRFMSE ARALTNFVGN GVATLVIARS EKALDTNRLQ RVLNGEVLPP
ATPEVAAEER GEGRGLDGPL PA