ID   PSTS_STAAS              Reviewed;         327 AA.
AC   Q6G9H1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Phosphate-binding protein PstS;
DE            Short=PBP;
DE   Flags: Precursor;
GN   Name=pstS; OrderedLocusNames=SAS1330;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in
CC       phosphate import. {ECO:0000250}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PstB),
CC       two transmembrane proteins (PstC and PstA) and a solute-binding protein
CC       (PstS). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
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DR   EMBL; BX571857; CAG43106.1; -; Genomic_DNA.
DR   RefSeq; WP_000759232.1; NC_002953.3.
DR   AlphaFoldDB; Q6G9H1; -.
DR   SMR; Q6G9H1; -.
DR   KEGG; sas:SAS1330; -.
DR   HOGENOM; CLU_026228_1_1_9; -.
DR   OMA; GTKHGTR; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042301; F:phosphate ion binding; IEA:InterPro.
DR   GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR024370; PBP_domain.
DR   InterPro; IPR011862; Phos-bd.
DR   Pfam; PF12849; PBP_like_2; 1.
DR   TIGRFAMs; TIGR02136; ptsS_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Phosphate transport;
KW   Signal; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..327
FT                   /note="Phosphate-binding protein PstS"
FT                   /id="PRO_0000281660"
FT   REGION          307..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   327 AA;  36117 MW;  FAFC54F55EA7C71A CRC64;
     MKKWQFVGTT ALGATLLLGA CGGGNGGSGN SDLKGEAKGD GSSTVAPIVE KLNEKWAQDH
     SDAKISAGQA GTGAGFQKFI AGDIDFADAS RPIKDEEKQK LQDKNIKYKE FKIAQDGVTV
     AVNKENDFVD ELDKQQLKAI YSGKAKTWKD VNSKWPDKKI NAVSPNSSHG TYDFFENEVM
     NKEDIKAEKN ADTNAIVSSV TKNKEGIGYF GYNFYVQNKD KLKEVKIKDE NGKATEPTKK
     TIQDNSYALS RPLFIYVNEK ALKDNKVMSE FIKFVLEDKG KAAEEAGYVA APEKTYKSQL
     DDLKAFIDKN QKSDDKKSDD KKSEDKK