ID   PSTB2_PECAS             Reviewed;         258 AA.
AC   Q6CYN3;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Phosphate import ATP-binding protein PstB 2 {ECO:0000255|HAMAP-Rule:MF_01702};
DE            EC=7.3.2.1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE   AltName: Full=ABC phosphate transporter 2 {ECO:0000255|HAMAP-Rule:MF_01702};
DE   AltName: Full=Phosphate-transporting ATPase 2 {ECO:0000255|HAMAP-Rule:MF_01702};
GN   Name=pstB2 {ECO:0000255|HAMAP-Rule:MF_01702}; OrderedLocusNames=ECA4474;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(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 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX950851; CAG77369.1; -; Genomic_DNA.
DR   RefSeq; WP_011095929.1; NC_004547.2.
DR   AlphaFoldDB; Q6CYN3; -.
DR   SMR; Q6CYN3; -.
DR   STRING; 218491.ECA4474; -.
DR   EnsemblBacteria; CAG77369; CAG77369; ECA4474.
DR   GeneID; 57211161; -.
DR   KEGG; eca:ECA4474; -.
DR   PATRIC; fig|218491.5.peg.4562; -.
DR   eggNOG; COG1117; Bacteria.
DR   HOGENOM; CLU_000604_1_22_6; -.
DR   OMA; TIDICRV; -.
DR   OrthoDB; 1416748at2; -.
DR   Proteomes; UP000007966; 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; Reference proteome; Translocase;
KW   Transport.
FT   CHAIN           1..258
FT                   /note="Phosphate import ATP-binding protein PstB 2"
FT                   /id="PRO_0000092818"
FT   DOMAIN          12..253
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
SQ   SEQUENCE   258 AA;  29117 MW;  FE9A46F371FB2693 CRC64;
     MSMTTETSTN KIQVRDLNFY YGKFHALKNI TLDIAANQVT AFIGPSGCGK STLLRTLNKM
     YQLYPEQRAE GDILLDGNNI LTDKQDIALL RAKVGMVFQK PTPFPMSIYD NIAFGVRLFE
     KLSRADMDER VQWALTKAAL WQETKDKLHQ SGYSLSGGQQ QRLCIARGIA IRPDVLLLDE
     PCSALDPIST GRIEELISEL KKDYTVVIVT HNMQQAARCS DHTAFMYLGE LIEFSDTDTL
     FTAPRQKQTE DYITGRYG