PSTS_ECOLI
ID PSTS_ECOLI Reviewed; 346 AA.
AC P0AG82; P06128; P76744; Q2M846;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Phosphate-binding protein PstS;
DE Short=PBP;
DE Flags: Precursor;
GN Name=pstS; Synonyms=phoS; OrderedLocusNames=b3728, JW3706;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=6321434; DOI=10.1128/jb.157.3.772-778.1984;
RA Surin B.P., Jans D.A., Fimmel A.L., Shaw D.C., Cox G.B., Rosenberg H.;
RT "Structural gene for the phosphate-repressible phosphate-binding protein of
RT Escherichia coli has its own promoter: complete nucleotide sequence of the
RT phoS gene.";
RL J. Bacteriol. 157:772-778(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=6365894; DOI=10.1128/jb.157.3.909-917.1984;
RA Magota K., Otsuji N., Miki T., Horiuchi T., Tsunasawa S., Kondo J.,
RA Sakiyama F., Amemura M., Morita T., Shinagawa H., Nakata A.;
RT "Nucleotide sequence of the phoS gene, the structural gene for the
RT phosphate-binding protein of Escherichia coli.";
RL J. Bacteriol. 157:909-917(1984).
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 26-37.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=2215649; DOI=10.1038/347402a0;
RA Luecke H., Quiocho F.A.;
RT "High specificity of a phosphate transport protein determined by hydrogen
RT bonds.";
RL Nature 347:402-406(1990).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF MUTANT ASN-81.
RX PubMed=9228942; DOI=10.1038/nsb0797-519;
RA Wang Z., Luecke H., Yao N., Quiocho F.A.;
RT "A low energy short hydrogen bond in very high resolution structures of
RT protein receptor-phosphate complexes.";
RL Nat. Struct. Biol. 4:519-522(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=9671506; DOI=10.1021/bi980428z;
RA Hirshberg M., Henrick K., Haire L.L., Vasisht N., Brune M., Corrie J.E.,
RA Webb M.R.;
RT "Crystal structure of phosphate binding protein labeled with a coumarin
RT fluorophore, a probe for inorganic phosphate.";
RL Biochemistry 37:10381-10385(1998).
CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in
CC phosphate import.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By phosphate deprivation. Positively regulated by PhoB and
CC negatively regulated by PhoR.
CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
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DR EMBL; K01992; AAA24378.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62079.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76751.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77560.1; -; Genomic_DNA.
DR PIR; A30277; BYECPR.
DR RefSeq; NP_418184.1; NC_000913.3.
DR RefSeq; WP_000867146.1; NZ_STEB01000015.1.
DR PDB; 1A40; X-ray; 1.70 A; A=26-346.
DR PDB; 1A54; X-ray; 1.60 A; A=26-346.
DR PDB; 1A55; X-ray; 2.40 A; A=26-346.
DR PDB; 1IXG; X-ray; 1.05 A; A=26-346.
DR PDB; 1IXH; X-ray; 0.98 A; A=26-346.
DR PDB; 1IXI; X-ray; 1.89 A; A=26-346.
DR PDB; 1OIB; X-ray; 2.40 A; A/B=26-346.
DR PDB; 1PBP; X-ray; 1.90 A; A=26-346.
DR PDB; 1QUI; X-ray; 1.90 A; A=26-346.
DR PDB; 1QUJ; X-ray; 1.90 A; A=26-346.
DR PDB; 1QUK; X-ray; 1.70 A; A=26-346.
DR PDB; 1QUL; X-ray; 1.70 A; A=26-346.
DR PDB; 2ABH; X-ray; 1.70 A; A=26-346.
DR PDBsum; 1A40; -.
DR PDBsum; 1A54; -.
DR PDBsum; 1A55; -.
DR PDBsum; 1IXG; -.
DR PDBsum; 1IXH; -.
DR PDBsum; 1IXI; -.
DR PDBsum; 1OIB; -.
DR PDBsum; 1PBP; -.
DR PDBsum; 1QUI; -.
DR PDBsum; 1QUJ; -.
DR PDBsum; 1QUK; -.
DR PDBsum; 1QUL; -.
DR PDBsum; 2ABH; -.
DR AlphaFoldDB; P0AG82; -.
DR SMR; P0AG82; -.
DR BioGRID; 4262139; 97.
DR ComplexPortal; CPX-4381; Phosphate ABC transporter complex.
DR DIP; DIP-48241N; -.
DR IntAct; P0AG82; 2.
DR STRING; 511145.b3728; -.
DR DrugBank; DB02831; Dihydrogenphosphate.
DR DrugBank; DB02799; N-[2-(1-maleimidyl)ethyl]-7-diethylaminocoumarin-3-carboxamide.
DR TCDB; 3.A.1.7.1; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P0AG82; -.
DR jPOST; P0AG82; -.
DR PaxDb; P0AG82; -.
DR PRIDE; P0AG82; -.
DR EnsemblBacteria; AAC76751; AAC76751; b3728.
DR EnsemblBacteria; BAE77560; BAE77560; BAE77560.
DR GeneID; 66672372; -.
DR GeneID; 948237; -.
DR KEGG; ecj:JW3706; -.
DR KEGG; eco:b3728; -.
DR PATRIC; fig|1411691.4.peg.2972; -.
DR EchoBASE; EB0727; -.
DR eggNOG; COG0226; Bacteria.
DR HOGENOM; CLU_034528_1_0_6; -.
DR InParanoid; P0AG82; -.
DR OMA; FPYPVYA; -.
DR PhylomeDB; P0AG82; -.
DR BioCyc; EcoCyc:PSTS-MON; -.
DR BioCyc; MetaCyc:PSTS-MON; -.
DR EvolutionaryTrace; P0AG82; -.
DR PRO; PR:P0AG82; -.
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:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042301; F:phosphate ion binding; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IC:ComplexPortal.
DR GO; GO:0006817; P:phosphate ion transport; IDA:EcoCyc.
DR GO; GO:0010921; P:regulation of phosphatase activity; IDA:EcoCyc.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR InterPro; IPR005673; ABC_phos-bd_PstS.
DR InterPro; IPR024370; PBP_domain.
DR Pfam; PF12849; PBP_like_2; 1.
DR PIRSF; PIRSF002756; PstS; 1.
DR TIGRFAMs; TIGR00975; 3a0107s03; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Periplasm; Phosphate transport;
KW Reference proteome; Signal; Stress response; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 26..346
FT /note="Phosphate-binding protein PstS"
FT /id="PRO_0000031848"
FT BINDING 34..36
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT BINDING 63
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT BINDING 81
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT BINDING 164..166
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1IXH"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1A55"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:1IXH"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1IXH"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:1IXH"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:1IXH"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:1IXH"
FT STRAND 94..108
FT /evidence="ECO:0007829|PDB:1IXH"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1A54"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:1IXH"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:1IXH"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1IXH"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:1IXH"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:1IXH"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1A40"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1IXH"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:1IXH"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:1IXH"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:1IXH"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1IXH"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1IXH"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:1IXH"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1IXH"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:1IXH"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:1OIB"
FT STRAND 276..288
FT /evidence="ECO:0007829|PDB:1IXH"
FT HELIX 292..308
FT /evidence="ECO:0007829|PDB:1IXH"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:1IXH"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:1IXH"
SQ SEQUENCE 346 AA; 37024 MW; 867DA7199C2C87ED CRC64;
MKVMRTTVAT VVAATLSMSA FSVFAEASLT GAGATFPAPV YAKWADTYQK ETGNKVNYQG
IGSSGGVKQI IANTVDFGAS DAPLSDEKLA QEGLFQFPTV IGGVVLAVNI PGLKSGELVL
DGKTLGDIYL GKIKKWDDEA IAKLNPGLKL PSQNIAVVRR ADGSGTSFVF TSYLAKVNEE
WKNNVGTGST VKWPIGLGGK GNDGIAAFVQ RLPGAIGYVE YAYAKQNNLA YTKLISADGK
PVSPTEENFA NAAKGADWSK TFAQDLTNQK GEDAWPITST TFILIHKDQK KPEQGTEVLK
FFDWAYKTGA KQANDLDYAS LPDSVVEQVR AAWKTNIKDS SGKPLY
