ID   PSTB_PSEPU              Reviewed;         277 AA.
AC   Q9Z411;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 98.
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};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PRS2000;
RX   PubMed=16232467; DOI=10.1016/s1389-1723(99)80031-0;
RA   Wu H., Kosaka H., Kato J., Kuroda A., Ikeda T., Takiguchi N., Ohtake H.;
RT   "Cloning and characterization of Pseudomonas putida genes encoding the
RT   phosphate-specific transport system.";
RL   J. Biosci. Bioeng. 87:273-279(1999).
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; AB017356; BAA75657.1; -; Genomic_DNA.
DR   PIR; T43868; T43868.
DR   AlphaFoldDB; Q9Z411; -.
DR   SMR; Q9Z411; -.
DR   STRING; 1240350.AMZE01000020_gene1430; -.
DR   eggNOG; COG1117; Bacteria.
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 inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Phosphate transport; Translocase; Transport.
FT   CHAIN           1..277
FT                   /note="Phosphate import ATP-binding protein PstB"
FT                   /id="PRO_0000092864"
FT   DOMAIN          31..272
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
SQ   SEQUENCE   277 AA;  30992 MW;  289A3D8F59E7506E CRC64;
     MQQDSHTHGI DMSALGRNKQ GLQLAEETVA IEVPGLSLFY GDKQALFDVS MNIPKQRVTA
     FIGPSGCGKS TLLRTFNRMN DLVDGCRVEG AINLYGNNIY RKGEDVAELR RRVGMVFQKP
     NPFPKTIYEN VVYGLRIQGI NKKRVLDEAV EWALKGAALW DEVKDRLHES ALGLSGGQQQ
     RLVIARTIAV EPEVLLLDEP CSALDPISTL KVEELIYELK SKYTIVIVTH NMQQAARVSD
     YTAFMYLGKL VEFGDTDTLF TNPAKKQTED YITGRYG