PSTB_SALTI
ID PSTB_SALTI Reviewed; 257 AA.
AC P63366; P58656; P58657;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
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};
GN OrderedLocusNames=STY3929, t3669;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01702}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC 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; AL513382; CAD03145.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71165.1; -; Genomic_DNA.
DR RefSeq; NP_458092.1; NC_003198.1.
DR RefSeq; WP_000063118.1; NZ_WSUR01000023.1.
DR AlphaFoldDB; P63366; -.
DR SMR; P63366; -.
DR STRING; 220341.16504780; -.
DR EnsemblBacteria; AAO71165; AAO71165; t3669.
DR GeneID; 66758143; -.
DR KEGG; stt:t3669; -.
DR KEGG; sty:STY3929; -.
DR PATRIC; fig|220341.7.peg.4009; -.
DR eggNOG; COG1117; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; TIDICRV; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
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; IPR015850; ABC_transpr_PstB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005670; Phosp_transpt1.
DR PANTHER; PTHR43423; PTHR43423; 1.
DR PANTHER; PTHR43423:SF3; PTHR43423:SF3; 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 inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Phosphate transport; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..257
FT /note="Phosphate import ATP-binding protein PstB"
FT /id="PRO_0000092872"
FT DOMAIN 11..252
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
SQ SEQUENCE 257 AA; 29016 MW; B8D122AE960F3F53 CRC64;
MSMVETAPSK IQVRDLNFYY GKFHALKNIN LDIAKNQVTA FIGPSGCGKS TLLRTFNKMY
SLYPEQRAEG EILLDGDNIL TNTQDIALLR AKVGMVFQKP TPFPMSIYDN IAFGVRLFEK
LSRADMDERV QWALTKAALW NETKDKLHQS GYSLSGGQQQ RLCIARGIAI RPEVLLLDEP
CSALDPISTG RIEELITELK QDYTVVIVTH NMQQAARCSD HTAFMYLGEL IEFSNTDDLF
TKPAKKQTED YITGRYG
