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CYSA_SALTI
ID   CYSA_SALTI              Reviewed;         364 AA.
AC   Q8Z4V6;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 136.
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};
GN   OrderedLocusNames=STY2678, t0417;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(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; AL513382; CAD07672.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68135.1; -; Genomic_DNA.
DR   RefSeq; NP_456976.1; NC_003198.1.
DR   RefSeq; WP_000021072.1; NZ_WSUR01000025.1.
DR   AlphaFoldDB; Q8Z4V6; -.
DR   SMR; Q8Z4V6; -.
DR   STRING; 220341.16503658; -.
DR   EnsemblBacteria; AAO68135; AAO68135; t0417.
DR   KEGG; stt:t0417; -.
DR   KEGG; sty:STY2678; -.
DR   PATRIC; fig|220341.7.peg.2715; -.
DR   eggNOG; COG1118; Bacteria.
DR   HOGENOM; CLU_000604_1_1_6; -.
DR   OMA; HLGWEIQ; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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   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   Pfam; PF00005; ABC_tran; 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..364
FT                   /note="Sulfate/thiosulfate import ATP-binding protein CysA"
FT                   /id="PRO_0000092290"
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   364 AA;  40850 MW;  7A95D914C1E7FDDA CRC64;
     MSIEIARIKK SFGRTQVLND ISLDIPSGQM VALLGPSGSG KTTLLRIIAG LEHQSSGHIR
     FHGTDVSRLH ARERKVGFVF QHYALFRHMT VFDNIAFGLT VLPRRDRPTA AAIKTKVTQL
     LEMVQLAHLA DRFPAQLSGG QKQRVALARA LAVEPQILLL DEPFGALDAQ VRKELRRWLR
     QLHEELKFTS VFVTHDQEEA TEVADRVVVM SQGNIEQADA PDRVWREPAT RFVLEFMGEV
     NRLTGTVRGG QFHVGAHRWP LGYTPAYQGP VDLFLRPWEV DISRRTSLDS PLPVQVIEAS
     PKGHYTQLVV QPLGWYHDPL TVVMAGDDVP QRGERLFVGL QNARLYHGDQ RIEPHEALAL
     AESA
 
 
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