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CYSA_XYLFT
ID   CYSA_XYLFT              Reviewed;         348 AA.
AC   Q87DT9;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Sulfate/thiosulfate import ATP-binding protein CysA {ECO:0000255|HAMAP-Rule:MF_01701};
DE            EC=7.3.2.3 {ECO:0000255|HAMAP-Rule:MF_01701};
DE   AltName: Full=Sulfate-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01701};
GN   Name=cysA {ECO:0000255|HAMAP-Rule:MF_01701}; OrderedLocusNames=PD_0591;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964;
RX   PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA   Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA   Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA   Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA   Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA   Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA   Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA   Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA   Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA   Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA   Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA   Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's disease
RT   and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex CysAWTP involved in
CC       sulfate/thiosulfate import. Responsible for energy coupling to the
CC       transport system. {ECO:0000255|HAMAP-Rule:MF_01701}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + sulfate(out) = ADP + H(+) + phosphate +
CC         sulfate(in); Xref=Rhea:RHEA:10192, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01701};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + thiosulfate(out) = ADP + H(+) + phosphate +
CC         thiosulfate(in); Xref=Rhea:RHEA:29871, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33542,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01701};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (CysA),
CC       two transmembrane proteins (CysT and CysW) and a solute-binding protein
CC       (CysP). {ECO:0000255|HAMAP-Rule:MF_01701}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01701}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01701}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       Sulfate/tungstate importer (TC 3.A.1.6) family. {ECO:0000255|HAMAP-
CC       Rule:MF_01701}.
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DR   EMBL; AE009442; AAO28464.1; -; Genomic_DNA.
DR   RefSeq; WP_011097711.1; NC_004556.1.
DR   AlphaFoldDB; Q87DT9; -.
DR   SMR; Q87DT9; -.
DR   EnsemblBacteria; AAO28464; AAO28464; PD_0591.
DR   GeneID; 58016137; -.
DR   KEGG; xft:PD_0591; -.
DR   HOGENOM; CLU_000604_1_1_6; -.
DR   OMA; HLGWEIQ; -.
DR   Proteomes; UP000002516; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0015419; F:ABC-type sulfate transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0102025; F:ABC-type thiosulfate transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd03296; ABC_CysA_sulfate_importer; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005666; Sulph_transpt1.
DR   InterPro; IPR024765; TOBE-like.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF12857; TOBE_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; SSF50331; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00968; 3a0106s01; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51237; CYSA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Sulfate transport; Translocase; Transport.
FT   CHAIN           1..348
FT                   /note="Sulfate/thiosulfate import ATP-binding protein CysA"
FT                   /id="PRO_0000092303"
FT   DOMAIN          3..237
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01701"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01701"
SQ   SEQUENCE   348 AA;  38771 MW;  0090423D30D94A61 CRC64;
     MGIRIQELRK QFEDFTALAG IDLDIRQGEL LALLGPSGSG KTTLLRIIAG LEHADAGRVL
     FGDEDATTMS VQARRVGFVF QHYALFKHMS VYENVAFGLR VRRGKARWPE SQISARVFEL
     LSLVQLDGLE QRYPMQLSGG QRQRVALARA LAIEPRVLLL DEPFGALDAQ VRRDLRRWLR
     EIHDRTGLTT VFVTHDQEEA LELADRVAIL NQGGIEQVAS PDEVYNRPSS PFVYSFVGAV
     NRLPGCVGAD GLEVAGIVLS CPPQLSGWGA VDLYVRPEDL VLDAQEGWSA IVLWSQRSGP
     RMRVRARLEH SAHEVEIELS SATDEYVEGQ KLRLIPRHYG VFFSESGS
 
 
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