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CYSA_ECOLI
ID   CYSA_ECOLI              Reviewed;         365 AA.
AC   P16676; P77693;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 195.
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=b2422, JW2415;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2188958; DOI=10.1128/jb.172.6.3351-3357.1990;
RA   Sirko A., Hryniewicz M.M., Hulanicka D.M., Boeck A.;
RT   "Sulfate and thiosulfate transport in Escherichia coli K-12: nucleotide
RT   sequence and expression of the cysTWAM gene cluster.";
RL   J. Bacteriol. 172:3351-3357(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   ALTERNATIVE MOLYBDATE TRANSPORT.
RX   PubMed=7665461; DOI=10.1128/jb.177.17.4857-4864.1995;
RA   Rosentel J.K., Healy F., Maupin-Furlow J.A., Lee J.H., Shanmugam K.T.;
RT   "Molybdate and regulation of mod (molybdate transport), fdhF, and hyc
RT   (formate hydrogenlyase) operons in Escherichia coli.";
RL   J. Bacteriol. 177:4857-4864(1995).
CC   -!- FUNCTION: Part of the ABC transporter complex CysAWTP involved in
CC       sulfate/thiosulfate import. Responsible for energy coupling to the
CC       transport system.
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   -!- INTERACTION:
CC       P16676; P07004: proA; NbExp=3; IntAct=EBI-556404, EBI-548584;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01701}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01701}.
CC   -!- MISCELLANEOUS: CysPTWAM system can also transport molybdate.
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; M32101; AAA23639.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75475.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16296.1; -; Genomic_DNA.
DR   PIR; E65016; QRECSA.
DR   RefSeq; NP_416917.1; NC_000913.3.
DR   RefSeq; WP_000021036.1; NZ_SSZK01000005.1.
DR   AlphaFoldDB; P16676; -.
DR   SMR; P16676; -.
DR   BioGRID; 4260755; 35.
DR   BioGRID; 851229; 1.
DR   ComplexPortal; CPX-4385; Sulfate/thiosulfate ABC transporter complex, cypP variant.
DR   ComplexPortal; CPX-4386; Sulfate/thiosulfate ABC transporter complex, sbp variant.
DR   DIP; DIP-9373N; -.
DR   IntAct; P16676; 4.
DR   STRING; 511145.b2422; -.
DR   TCDB; 3.A.1.6.1; the atp-binding cassette (abc) superfamily.
DR   jPOST; P16676; -.
DR   PaxDb; P16676; -.
DR   PRIDE; P16676; -.
DR   EnsemblBacteria; AAC75475; AAC75475; b2422.
DR   EnsemblBacteria; BAA16296; BAA16296; BAA16296.
DR   GeneID; 946889; -.
DR   KEGG; ecj:JW2415; -.
DR   KEGG; eco:b2422; -.
DR   PATRIC; fig|1411691.4.peg.4309; -.
DR   EchoBASE; EB0180; -.
DR   eggNOG; COG1118; Bacteria.
DR   HOGENOM; CLU_000604_1_1_6; -.
DR   InParanoid; P16676; -.
DR   OMA; HLGWEIQ; -.
DR   PhylomeDB; P16676; -.
DR   BioCyc; EcoCyc:CYSA-MON; -.
DR   BioCyc; MetaCyc:CYSA-MON; -.
DR   PRO; PR:P16676; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0035796; C:ATP-binding cassette (ABC) transporter complex, transmembrane substrate-binding subunit-containing; IC:ComplexPortal.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
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; ISM:EcoCyc.
DR   GO; GO:1902358; P:sulfate transmembrane transport; IC:ComplexPortal.
DR   GO; GO:0008272; P:sulfate transport; IBA:GO_Central.
DR   GO; GO:0015709; P:thiosulfate transport; IC:ComplexPortal.
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   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   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Sulfate transport; Translocase;
KW   Transport.
FT   CHAIN           1..365
FT                   /note="Sulfate/thiosulfate import ATP-binding protein CysA"
FT                   /id="PRO_0000092265"
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"
FT   CONFLICT        136..137
FT                   /note="QL -> HV (in Ref. 1; AAA23639)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   365 AA;  41059 MW;  B5FCCA346EDF2788 CRC64;
     MSIEIANIKK SFGRTQVLND ISLDIPSGQM VALLGPSGSG KTTLLRIIAG LEHQTSGHIR
     FHGTDVSRLH ARDRKVGFVF QHYALFRHMT VFDNIAFGLT VLPRRERPNA AAIKAKVTKL
     LEMVQLAHLA DRYPAQLSGG QKQRVALARA LAVEPQILLL DEPFGALDAQ VRKELRRWLR
     QLHEELKFTS VFVTHDQEEA TEVADRVVVM SQGNIEQADA PDQVWREPAT RFVLEFMGEV
     NRLQGTIRGG QFHVGAHRWP LGYTPAYQGP VDLFLRPWEV DISRRTSLDS PLPVQVLEAS
     PKGHYTQLVV QPLGWYNEPL TVVMHGDDAP QRGERLFVGL QHARLYNGDE RIETRDEELA
     LAQSA
 
 
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