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CYSP_ECOLI
ID   CYSP_ECOLI              Reviewed;         338 AA.
AC   P16700;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Thiosulfate-binding protein;
DE   Flags: Precursor;
GN   Name=cysP; OrderedLocusNames=b2425, JW2418;
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=2188959; DOI=10.1128/jb.172.6.3358-3366.1990;
RA   Hryniewicz M.M., Sirko A., Palucha A., Boeck A., Hulanicka D.M.;
RT   "Sulfate and thiosulfate transport in Escherichia coli K-12: identification
RT   of a gene encoding a novel protein involved in thiosulfate binding.";
RL   J. Bacteriol. 172:3358-3366(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   PROTEIN SEQUENCE OF 26-37.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
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.
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; M32101; AAA23636.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75478.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16299.1; -; Genomic_DNA.
DR   PIR; A35403; JGECT.
DR   RefSeq; NP_416920.1; NC_000913.3.
DR   RefSeq; WP_000290230.1; NZ_LN832404.1.
DR   AlphaFoldDB; P16700; -.
DR   SMR; P16700; -.
DR   BioGRID; 4263209; 23.
DR   ComplexPortal; CPX-4385; Sulfate/thiosulfate ABC transporter complex, cypP variant.
DR   DIP; DIP-9384N; -.
DR   IntAct; P16700; 6.
DR   STRING; 511145.b2425; -.
DR   TCDB; 3.A.1.6.1; the atp-binding cassette (abc) superfamily.
DR   SWISS-2DPAGE; P16700; -.
DR   jPOST; P16700; -.
DR   PaxDb; P16700; -.
DR   PRIDE; P16700; -.
DR   EnsemblBacteria; AAC75478; AAC75478; b2425.
DR   EnsemblBacteria; BAA16299; BAA16299; BAA16299.
DR   GeneID; 946883; -.
DR   KEGG; ecj:JW2418; -.
DR   KEGG; eco:b2425; -.
DR   PATRIC; fig|1411691.4.peg.4306; -.
DR   EchoBASE; EB0192; -.
DR   eggNOG; COG4150; Bacteria.
DR   HOGENOM; CLU_055615_0_1_6; -.
DR   InParanoid; P16700; -.
DR   OMA; PKNIHSW; -.
DR   PhylomeDB; P16700; -.
DR   BioCyc; EcoCyc:CYSP-MON; -.
DR   BioCyc; MetaCyc:CYSP-MON; -.
DR   PRO; PR:P16700; -.
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:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0043199; F:sulfate binding; IDA:EcoCyc.
DR   GO; GO:0036173; F:thiosulfate binding; IDA:EcoCyc.
DR   GO; GO:1902358; P:sulfate transmembrane transport; IC:ComplexPortal.
DR   GO; GO:0008272; P:sulfate transport; IMP:EcoCyc.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IMP:EcoCyc.
DR   GO; GO:0015709; P:thiosulfate transport; IMP:EcoCyc.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Periplasm; Reference proteome; Signal;
KW   Sulfate transport; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:9298646"
FT   CHAIN           26..338
FT                   /note="Thiosulfate-binding protein"
FT                   /id="PRO_0000031681"
SQ   SEQUENCE   338 AA;  37615 MW;  79BCD531AFA01DC1 CRC64;
     MAVNLLKKNS LALVASLLLA GHVQATELLN SSYDVSRELF AALNPPFEQQ WAKDNGGDKL
     TIKQSHAGSS KQALAILQGL KADVVTYNQV TDVQILHDKG KLIPADWQSR LPNNSSPFYS
     TMGFLVRKGN PKNIHDWNDL VRSDVKLIFP NPKTSGNARY TYLAAWGAAD KADGGDKGKT
     EQFMTQFLKN VEVFDTGGRG ATTTFAERGL GDVLISFESE VNNIRKQYEA QGFEVVIPKT
     NILAEFPVAW VDKNVQANGT EKAAKAYLNW LYSPQAQTII TDYYYRVNNP EVMDKLKDKF
     PQTELFRVED KFGSWPEVMK THFTSGGELD KLLAAGRN
 
 
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