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Database: UniProt
Entry: E0SES9_DICD3
LinkDB: E0SES9_DICD3
Original site: E0SES9_DICD3 
ID   E0SES9_DICD3            Unreviewed;       428 AA.
AC   E0SES9;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=C4-dicarboxylate transport protein {ECO:0000256|HAMAP-Rule:MF_01300};
GN   Name=dctA {ECO:0000256|HAMAP-Rule:MF_01300,
GN   ECO:0000313|EMBL:ADM96332.1};
GN   OrderedLocusNames=Dda3937_01995 {ECO:0000313|EMBL:ADM96332.1};
OS   Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=198628 {ECO:0000313|EMBL:ADM96332.1, ECO:0000313|Proteomes:UP000006859};
RN   [1] {ECO:0000313|EMBL:ADM96332.1, ECO:0000313|Proteomes:UP000006859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3937 {ECO:0000313|EMBL:ADM96332.1,
RC   ECO:0000313|Proteomes:UP000006859};
RX   PubMed=21217001; DOI=10.1128/JB.01513-10;
RA   Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA   Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA   Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA   Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA   Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA   Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA   Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA   Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA   Blattner F.R., Keen N.T., Perna N.T.;
RT   "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL   J. Bacteriol. 193:2076-2077(2011).
CC   -!- FUNCTION: Responsible for the transport of dicarboxylates such as
CC       succinate, fumarate, and malate from the periplasm across the membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_01300}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01300}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01300}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC       (DAACS) (TC 2.A.23) family. {ECO:0000256|ARBA:ARBA00006148,
CC       ECO:0000256|HAMAP-Rule:MF_01300}.
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DR   EMBL; CP002038; ADM96332.1; -; Genomic_DNA.
DR   RefSeq; WP_013315821.1; NC_014500.1.
DR   AlphaFoldDB; E0SES9; -.
DR   STRING; 198628.Dda3937_01995; -.
DR   GeneID; 9731501; -.
DR   KEGG; ddd:Dda3937_01995; -.
DR   PATRIC; fig|198628.6.peg.122; -.
DR   eggNOG; COG1301; Bacteria.
DR   HOGENOM; CLU_019375_7_0_6; -.
DR   OrthoDB; 9766690at2; -.
DR   Proteomes; UP000006859; 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 {ECO:0000256|HAMAP-Rule:MF_01300};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01300};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01300};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006859};
KW   Symport {ECO:0000256|ARBA:ARBA00022847, ECO:0000256|HAMAP-Rule:MF_01300};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01300};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01300};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01300}.
FT   TRANSMEM        9..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01300"
FT   TRANSMEM        47..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01300"
FT   TRANSMEM        76..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01300"
FT   TRANSMEM        141..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01300"
FT   TRANSMEM        184..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01300"
FT   TRANSMEM        220..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01300"
FT   TRANSMEM        326..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01300"
FT   TRANSMEM        350..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01300"
SQ   SEQUENCE   428 AA;  45233 MW;  C675A8A89E5E70FF CRC64;
     MKKSIFKSLY FQVLAAITIG ILLGHFYPAL GQQMQPLGDG FVKLIKMVIA PVIFCTVVTG
     IAGMESMKAV GRTGAVALLY FEVVSTLALI IGLVVVNVLQ PGAGMNVDPA ALNVAAVANY
     ATEAGKQGVV PFLMDVIPSS VIGAFASGNI LQVLLFAVMF GFALHRLGDK GVLIFDVIES
     FSKVIFGIIN MIMRLAPLGA FGAMAFTIGK YGVGTLVQLG QLIICFYITC ILFVVLVLGS
     IARATGFSIF KFIRYIREEL LIVLGTSSSE SALPRMLEKM EKLGCKKSVV GLVIPTGYSF
     NLDGTSIYLT MAAVFIAQAT NSHMDIWHQI TLLVVLLLSS KGAAGVTGSG FIVLAATISA
     VGHLPLAGLA LILGIDRFMS EARALTNLVG NGVATVVVAK WCKQLDSKQM NDVLSGRNDG
     PAAESRPS
//
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