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PSTB_STAAS
ID   PSTB_STAAS              Reviewed;         283 AA.
AC   Q6G9H4;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Phosphate import ATP-binding protein PstB {ECO:0000255|HAMAP-Rule:MF_01702};
DE            EC=7.3.2.1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE   AltName: Full=ABC phosphate transporter {ECO:0000255|HAMAP-Rule:MF_01702};
DE   AltName: Full=Phosphate-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01702};
GN   Name=pstB {ECO:0000255|HAMAP-Rule:MF_01702}; OrderedLocusNames=SAS1327;
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. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01702}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in);
CC         Xref=Rhea:RHEA:24440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01702};
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:0000255|HAMAP-Rule:MF_01702}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01702};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01702}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate
CC       importer (TC 3.A.1.7) family. {ECO:0000255|HAMAP-Rule:MF_01702}.
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DR   EMBL; BX571857; CAG43103.1; -; Genomic_DNA.
DR   RefSeq; WP_000079447.1; NC_002953.3.
DR   AlphaFoldDB; Q6G9H4; -.
DR   SMR; Q6G9H4; -.
DR   KEGG; sas:SAS1327; -.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; TIDICRV; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015415; F:ATPase-coupled phosphate ion transmembrane transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd03260; ABC_PstB_phosphate_transporter; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005670; Phosp_transpt1.
DR   PANTHER; PTHR43423; PTHR43423; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00972; 3a0107s01c2; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51238; PSTB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Phosphate transport; Translocase; Transport.
FT   CHAIN           1..283
FT                   /note="Phosphate import ATP-binding protein PstB"
FT                   /id="PRO_0000092881"
FT   DOMAIN          37..278
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         69..76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
SQ   SEQUENCE   283 AA;  32154 MW;  ED50487D8362262D CRC64;
     MAQTLAQTKQ ISQSHTFDVS QSHHKTPDDT NSHSVIYSTQ NLDLWYGENH ALQNINLDIY
     ENQITAIIGP SGCGKSTYIK TLNRMVELVP SVKTAGKILY RDQDIFDQKY SKEQLRTNVG
     MVFQQPNPFP KSIYDNITYG PKIHGIKNKK VLDEIVEKSL RGAAIWDELK DRLHTNAYSL
     SGGQQQRVCI ARCLAIEPEV ILMDEPTSAL DPISTLRVEE LVQELKEKYT IIMVTHNMQQ
     AARVSDKTAF FLNGYVNEYD DTDKIFSNPS NKKTEDYISG RFG
 
 
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