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CYSP_SALTY
ID   CYSP_SALTY              Reviewed;         338 AA.
AC   P41031;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Thiosulfate-binding protein;
DE   Flags: Precursor;
GN   Name=cysP; OrderedLocusNames=STM2444;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1909324; DOI=10.1128/jb.173.18.5876-5886.1991;
RA   Hryniewicz M.M., Kredich N.M.;
RT   "The cysP promoter of Salmonella typhimurium: characterization of two
RT   binding sites for CysB protein, studies of in vivo transcription
RT   initiation, and demonstration of the anti-inducer effects of thiosulfate.";
RL   J. Bacteriol. 173:5876-5886(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1)
CC       involved in sulfate/thiosulfate import. This protein specifically binds
CC       thiosulfate and is involved in its transmembrane transport (By
CC       similarity). {ECO:0000250}.
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:0000305}.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the prokaryotic sulfate-binding protein family.
CC       {ECO:0000305}.
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DR   EMBL; AE006468; AAL21338.1; -; Genomic_DNA.
DR   RefSeq; NP_461379.1; NC_003197.2.
DR   RefSeq; WP_000290275.1; NC_003197.2.
DR   AlphaFoldDB; P41031; -.
DR   SMR; P41031; -.
DR   STRING; 99287.STM2444; -.
DR   PaxDb; P41031; -.
DR   PRIDE; P41031; -.
DR   EnsemblBacteria; AAL21338; AAL21338; STM2444.
DR   GeneID; 1253966; -.
DR   KEGG; stm:STM2444; -.
DR   PATRIC; fig|99287.12.peg.2582; -.
DR   HOGENOM; CLU_055615_0_1_6; -.
DR   OMA; PKNIHSW; -.
DR   PhylomeDB; P41031; -.
DR   BioCyc; SENT99287:STM2444-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:1901681; F:sulfur compound binding; IEA:InterPro.
DR   GO; GO:1902358; P:sulfate transmembrane transport; IEA:InterPro.
DR   CDD; cd01005; PBP2_CysP; 1.
DR   InterPro; IPR000957; Sulphate/thiosulphate-bd_CS.
DR   InterPro; IPR034408; Sulphate/thiosulphate_BS.
DR   InterPro; IPR005669; Thiosulph/SO4-bd.
DR   PANTHER; PTHR30368; PTHR30368; 1.
DR   TIGRFAMs; TIGR00971; 3a0106s03; 1.
DR   PROSITE; PS00401; PROK_SULFATE_BIND_1; 1.
DR   PROSITE; PS00757; PROK_SULFATE_BIND_2; 1.
PE   3: Inferred from homology;
KW   Periplasm; Reference proteome; Signal; Sulfate transport; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..338
FT                   /note="Thiosulfate-binding protein"
FT                   /id="PRO_0000031682"
FT   CONFLICT        110
FT                   /note="R -> L (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143..145
FT                   /note="SDV -> FDL (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   338 AA;  37583 MW;  3BB30B559122DAEF CRC64;
     MAVNLLKKRP LTLAAMLLLA GQAQATELLN SSYDVSRELF AALNPPFEQQ WAKDNGGDKL
     TIKQSHAGSS KQALAILQGL KADVVTYNQV TDVQILHDKG KLIPADWQSR LPNNSSPFYS
     TMGFLVRKGN PKNIHDWSDL VRSDVKLIFP NPKTSGNARY TYLAAWGAAD NADGGDKAKT
     EQFMTQFLKN VEVFDTGGRG ATTTFAERGL GDVLISFESE VNNIRKQYEA QGFEVVIPKT
     NILAEFPVAW VDKNVQANGT EKAAKAYLNW LYSPQAQTII THYYYRVNNP EIMGKQADKF
     PQTELFRVEE KFGSWPEVMK THFASGGELD KLLAAGRK
 
 
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