PSTB_ECOLI
ID PSTB_ECOLI Reviewed; 257 AA.
AC P0AAH0; P07655; Q2M843;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
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}; Synonyms=phoT;
GN OrderedLocusNames=b3725, JW3703;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2993631; DOI=10.1016/0022-2836(85)90377-8;
RA Amemura M., Makino K., Shinagawa H., Kobayashi A., Nakata A.;
RT "Nucleotide sequence of the genes involved in phosphate transport and
RT regulation of the phosphate regulon in Escherichia coli.";
RL J. Mol. Biol. 184:241-250(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3881386; DOI=10.1128/jb.161.1.189-198.1985;
RA Surin B.P., Rosenberg H., Cox G.B.;
RT "Phosphate-specific transport system of Escherichia coli: nucleotide
RT sequence and gene-polypeptide relationships.";
RL J. Bacteriol. 161:189-198(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-11, CHARACTERIZATION, AND MUTAGENESIS OF GLY-48 AND
RP LYS-49.
RC STRAIN=BL21-DE3;
RX PubMed=8682808; DOI=10.1128/jb.178.13.3974-3977.1996;
RA Chan F.-Y., Torriani A.;
RT "PstB protein of the phosphate-specific transport system of Escherichia
RT coli is an ATPase.";
RL J. Bacteriol. 178:3974-3977(1996).
CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in
CC phosphate import. Responsible for energy coupling to the transport
CC system.
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; Peripheral membrane protein.
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; X02723; CAA26509.1; -; Genomic_DNA.
DR EMBL; K01992; AAA24381.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62076.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76748.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77563.1; -; Genomic_DNA.
DR PIR; A30382; BVECZB.
DR RefSeq; NP_418181.1; NC_000913.3.
DR RefSeq; WP_000063125.1; NZ_STEB01000015.1.
DR AlphaFoldDB; P0AAH0; -.
DR SMR; P0AAH0; -.
DR BioGRID; 4262135; 10.
DR ComplexPortal; CPX-4381; Phosphate ABC transporter complex.
DR DIP; DIP-47851N; -.
DR IntAct; P0AAH0; 28.
DR STRING; 511145.b3725; -.
DR TCDB; 3.A.1.7.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AAH0; -.
DR PaxDb; P0AAH0; -.
DR PRIDE; P0AAH0; -.
DR EnsemblBacteria; AAC76748; AAC76748; b3725.
DR EnsemblBacteria; BAE77563; BAE77563; BAE77563.
DR GeneID; 66672375; -.
DR GeneID; 948240; -.
DR KEGG; ecj:JW3703; -.
DR KEGG; eco:b3725; -.
DR PATRIC; fig|1411691.4.peg.2975; -.
DR EchoBASE; EB0776; -.
DR eggNOG; COG1117; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR InParanoid; P0AAH0; -.
DR OMA; TIDICRV; -.
DR PhylomeDB; P0AAH0; -.
DR BioCyc; EcoCyc:PSTB-MON; -.
DR BioCyc; MetaCyc:PSTB-MON; -.
DR PRO; PR:P0AAH0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
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; IDA:EcoCyc.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006817; P:phosphate ion transport; IDA:EcoCyc.
DR GO; GO:0010921; P:regulation of phosphatase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Membrane; Nucleotide-binding; Phosphate transport; Reference proteome;
KW Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8682808"
FT CHAIN 2..257
FT /note="Phosphate import ATP-binding protein PstB"
FT /id="PRO_0000092810"
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"
FT MUTAGEN 48
FT /note="G->I: Loss of phosphate transport."
FT /evidence="ECO:0000269|PubMed:8682808"
FT MUTAGEN 49
FT /note="K->Q: Loss of phosphate transport."
FT /evidence="ECO:0000269|PubMed:8682808"
SQ SEQUENCE 257 AA; 29027 MW; 15A09F9DC3EB013A CRC64;
MSMVETAPSK IQVRNLNFYY GKFHALKNIN LDIAKNQVTA FIGPSGCGKS TLLRTFNKMF
ELYPEQRAEG EILLDGDNIL TNSQDIALLR AKVGMVFQKP TPFPMSIYDN IAFGVRLFEK
LSRADMDERV QWALTKAALW NETKDKLHQS GYSLSGGQQQ RLCIARGIAI RPEVLLLDEP
CSALDPISTG RIEELITELK QDYTVVIVTH NMQQAARCSD HTAFMYLGEL IEFSNTDDLF
TKPAKKQTED YITGRYG
