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DCTA_XANCP
ID   DCTA_XANCP              Reviewed;         448 AA.
AC   Q8P5J5;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=C4-dicarboxylate transport protein {ECO:0000255|HAMAP-Rule:MF_01300};
GN   Name=dctA {ECO:0000255|HAMAP-Rule:MF_01300}; OrderedLocusNames=XCC3346;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; AE008922; AAM42616.1; -; Genomic_DNA.
DR   RefSeq; NP_638692.1; NC_003902.1.
DR   RefSeq; WP_011038444.1; NC_003902.1.
DR   AlphaFoldDB; Q8P5J5; -.
DR   SMR; Q8P5J5; -.
DR   STRING; 340.xcc-b100_0852; -.
DR   EnsemblBacteria; AAM42616; AAM42616; XCC3346.
DR   GeneID; 58012122; -.
DR   KEGG; xcc:XCC3346; -.
DR   PATRIC; fig|190485.4.peg.3578; -.
DR   eggNOG; COG1301; Bacteria.
DR   HOGENOM; CLU_019375_7_0_6; -.
DR   OMA; QATNTPM; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015138; F:fumarate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015366; F:malate:proton symporter activity; IBA:GO_Central.
DR   GO; GO:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0070778; P:L-aspartate transmembrane transport; IBA:GO_Central.
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 inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..448
FT                   /note="C4-dicarboxylate transport protein"
FT                   /id="PRO_0000202114"
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        51..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        138..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        161..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        198..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   TRANSMEM        230..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01300"
FT   REGION          428..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  47406 MW;  42A5B1F97836F279 CRC64;
     MHISKPAGPL PAPVPFYRQL YFQVVVAIVL GALLGHFEPA FAESLKPLGD AFIKLVKMII
     APVIFLTIVT GIAGMTHLKT VGRVFAKSMT YFLFFSTLAL IVGMVVAHVV QPGAGMNINP
     AELDQSAVNT YVQKSHELSL VGFLMDIIPA TLISAFVDGN ILQVLFVAVL FGIALALVGE
     RGRPVLSFLE ALTAPVFRLV HMLMKAAPIG AFGAIAFTIG KYGVESLVNL AWLVGSFYLT
     SLFFVLVILG IVCRLCGFSV LKLIRYLKAE LLLVLGTSSS ESALPSLMEK MEKAGCEKSV
     VGLVVPTGYS FNLDGTNIYM TLAALFIAQA TNVDLTLGQQ ITLLAVAMLS SKGAAGVTGA
     GFITLAATLS VVPDVPVAGM ALILGVDRFM SECRSLTNFI GNAVATVVVS RWENALDRDQ
     LSLALDGRAP PLQAPVPPPD AVAPVSAR
 
 
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