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CYSA_XANAC
ID   CYSA_XANAC              Reviewed;         343 AA.
AC   Q8PNN4;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 129.
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=XAC1020;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
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: 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM35903.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008923; AAM35903.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003490451.1; NC_003919.1.
DR   AlphaFoldDB; Q8PNN4; -.
DR   SMR; Q8PNN4; -.
DR   STRING; 190486.XAC1020; -.
DR   EnsemblBacteria; AAM35903; AAM35903; XAC1020.
DR   GeneID; 66910205; -.
DR   KEGG; xac:XAC1020; -.
DR   eggNOG; COG1118; Bacteria.
DR   HOGENOM; CLU_000604_1_1_6; -.
DR   OMA; HLGWEIQ; -.
DR   Proteomes; UP000000576; 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; IPR041193; CysA_C.
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; PF17850; CysA_C_terminal; 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..343
FT                   /note="Sulfate/thiosulfate import ATP-binding protein CysA"
FT                   /id="PRO_0000092300"
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   343 AA;  38060 MW;  C4C4D28B50B99ADF CRC64;
     MGIRIHRLRK QFETFTALDN IDLEVRQGEL LALLGPSGSG KTTLLRIMAG LEHADGGQVL
     FGDEDATRMS VQSRRVGFVF QHYALFKHMD VFENIAFGLR VRRGNARWAE ARIRARVEEL
     LALVQLQGLE QRYPTQLSGG QRQRVALARA LAIEPRVLLL DEPFGALDAQ VRRDLRRWLR
     ELHERTGLTT VFVTHDQEEA LELADRVAIL NRGRIEQLDT PAMIYDKPAS PFVYSFVGAV
     NRIPGVLAQG QIQVAGHALP LANAALAAGP VEVYVRPEDL VPDQAGWPAT VAWSQRSGSR
     LRLRATLEPS GNEVEVELPA SAGSFQPGQQ VRLAARQYGI FPA
 
 
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