PHOU_ECOLI
ID PHOU_ECOLI Reviewed; 241 AA.
AC P0A9K7; P07656; Q2M842;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phosphate-specific transport system accessory protein PhoU;
DE Short=Pst system accessory protein PhoU;
DE AltName: Full=Negative regulator of Pho regulon;
GN Name=phoU; Synonyms=nmpA; OrderedLocusNames=b3724, JW3702;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-241.
RC STRAIN=K12;
RX PubMed=3034860; DOI=10.1128/jb.169.6.2579-2590.1987;
RA Schnetz K., Toloczyki C., Rak B.;
RT "Beta-glucoside (bgl) operon of Escherichia coli K-12: nucleotide sequence,
RT genetic organization, and possible evolutionary relationship to regulatory
RT components of two Bacillus subtilis genes.";
RL J. Bacteriol. 169:2579-2590(1987).
RN [7]
RP PROTEIN SEQUENCE OF 1-22, AND SUBCELLULAR LOCATION.
RX PubMed=3536855; DOI=10.1128/jb.168.2.631-635.1986;
RA Surin B.P., Dixon N.E., Rosenberg H.;
RT "Purification of the phoU protein, a negative regulator of the pho regulon
RT of Escherichia coli K-12.";
RL J. Bacteriol. 168:631-635(1986).
RN [8]
RP FUNCTION AS REPRESSOR OF PHO REGULON.
RX PubMed=6310121; DOI=10.1016/s0022-2836(83)80297-6;
RA Shinagawa H., Makino K., Nakata A.;
RT "Regulation of the pho regulon in Escherichia coli K-12. Genetic and
RT physiological regulation of the positive regulatory gene phoB.";
RL J. Mol. Biol. 168:477-488(1983).
RN [9]
RP SUGGESTION OF FUNCTION AS A REPRESSOR OF PHOB, AND INDUCTION.
RX PubMed=6090402; DOI=10.1128/jb.159.3.979-985.1984;
RA Nakata A., Amemura M., Shinagawa H.;
RT "Regulation of the phosphate regulon in Escherichia coli K-12: regulation
RT of the negative regulatory gene phoU and identification of the gene
RT product.";
RL J. Bacteriol. 159:979-985(1984).
RN [10]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / K10;
RX PubMed=1459954; DOI=10.1128/jb.174.24.8057-8064.1992;
RA Muda M., Rao N.N., Torriani A.;
RT "Role of PhoU in phosphate transport and alkaline phosphatase regulation.";
RL J. Bacteriol. 174:8057-8064(1992).
RN [11]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=8226621; DOI=10.1128/jb.175.21.6797-6809.1993;
RA Steed P.M., Wanner B.L.;
RT "Use of the rep technique for allele replacement to construct mutants with
RT deletions of the pstSCAB-phoU operon: evidence of a new role for the PhoU
RT protein in the phosphate regulon.";
RL J. Bacteriol. 175:6797-6809(1993).
RN [12]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12147514; DOI=10.1128/aem.68.8.4107-4110.2002;
RA Morohoshi T., Maruo T., Shirai Y., Kato J., Ikeda T., Takiguchi N.,
RA Ohtake H., Kuroda A.;
RT "Accumulation of inorganic polyphosphate in phoU mutants of Escherichia
RT coli and Synechocystis sp. strain PCC6803.";
RL Appl. Environ. Microbiol. 68:4107-4110(2002).
RN [13]
RP TRANSCRIPT ANALYSIS, AND OPERON STRUCTURE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12471449; DOI=10.1007/s00438-002-0764-4;
RA Aguena M., Yagil E., Spira B.;
RT "Transcriptional analysis of the pst operon of Escherichia coli.";
RL Mol. Genet. Genomics 268:518-524(2002).
RN [14]
RP FUNCTION IN TOLERANCE TO ANTIBIOTICS AND VARIOUS STRESSES, DISRUPTION
RP PHENOTYPE, AND POTENTIAL DRUG TARGET.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17420206; DOI=10.1128/aac.00052-07;
RA Li Y., Zhang Y.;
RT "PhoU is a persistence switch involved in persister formation and tolerance
RT to multiple antibiotics and stresses in Escherichia coli.";
RL Antimicrob. Agents Chemother. 51:2092-2099(2007).
RN [15]
RP INDUCTION.
RX PubMed=18031348; DOI=10.1111/j.1574-6968.2007.00965.x;
RA Baek J.H., Kang Y.J., Lee S.Y.;
RT "Transcript and protein level analyses of the interactions among PhoB,
RT PhoR, PhoU and CreC in response to phosphate starvation in Escherichia
RT coli.";
RL FEMS Microbiol. Lett. 277:254-259(2007).
RN [16]
RP REVIEW.
RX PubMed=18248418; DOI=10.1111/j.1574-6976.2008.00101.x;
RA Lamarche M.G., Wanner B.L., Crepin S., Harel J.;
RT "The phosphate regulon and bacterial virulence: a regulatory network
RT connecting phosphate homeostasis and pathogenesis.";
RL FEMS Microbiol. Rev. 32:461-473(2008).
RN [17]
RP DISRUPTION PHENOTYPE, AND EFFECT OF MUTATIONS ON REPRESSION OF AP ACTIVITY.
RX PubMed=19047379; DOI=10.1128/aem.01046-08;
RA Rice C.D., Pollard J.E., Lewis Z.T., McCleary W.R.;
RT "Employment of a promoter-swapping technique shows that PhoU modulates the
RT activity of the PstSCAB2 ABC transporter in Escherichia coli.";
RL Appl. Environ. Microbiol. 75:573-582(2009).
RN [18]
RP REVIEW.
RX PubMed=20171928; DOI=10.1016/j.mib.2010.01.014;
RA Hsieh Y.J., Wanner B.L.;
RT "Global regulation by the seven-component Pi signaling system.";
RL Curr. Opin. Microbiol. 13:198-203(2010).
CC -!- FUNCTION: Part of the phosphate (Pho) regulon, which plays a key role
CC in phosphate homeostasis. Encoded together with proteins of the
CC phosphate-specific transport (Pst) system in the polycistronic pstSCAB-
CC phoU operon. PhoU is essential for the repression of the Pho regulon at
CC high phosphate conditions. In this role, it may bind, possibly as a
CC chaperone, to PhoR, PhoB or a PhoR-PhoB complex to promote
CC dephosphorylation of phospho-PhoB, or inhibit formation of the PhoR-
CC PhoB transitory complex. Is also part of complex networks important for
CC bacterial virulence, tolerance to antibiotics and stress response.
CC {ECO:0000269|PubMed:17420206, ECO:0000269|PubMed:6310121}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3536855}.
CC -!- INDUCTION: Expressed at higher levels under excess phosphate culture
CC conditions (PubMed:6090402). Induced by phosphate starvation via the
CC PhoR/PhoB two-component regulatory system (PubMed:18031348).
CC {ECO:0000269|PubMed:18031348, ECO:0000269|PubMed:6090402}.
CC -!- DISRUPTION PHENOTYPE: Produces high level of alkaline phosphatase (AP)
CC when grown with excess phosphate (PubMed:1459954). No effect on
CC phosphate uptake, but particular deletion mutants have a severe growth
CC defect, which is largely alleviated by a compensatory mutation in the
CC pstSCAB genes or in the phoRB operon (PubMed:8226621). Accumulates high
CC levels of polyP, approximately 400 nmol of phosphate residues/mg of
CC protein (PubMed:12147514). Higher susceptibility to a diverse range of
CC antibiotics including ampicillin, norfloxacin and gentamicin, and
CC stresses such as starvation, acid pH, heat, peroxide, weak acids and
CC energy inhibitors, especially in stationary phase (PubMed:17420206).
CC Metabolically hyperactive status of the cell showing increased
CC expression of energy production genes, flagella and chemotaxis genes,
CC and a defect in persister formation (PubMed:17420206). Cells transport
CC phosphate via PstSCAB transporter system at approximately 20% higher
CC rate and accumulate higher levels of the transporter and about 50% more
CC phosphate in 12 minutes than wild-type cells in phosphate-replete
CC medium (PubMed:19047379). {ECO:0000269|PubMed:12147514,
CC ECO:0000269|PubMed:1459954, ECO:0000269|PubMed:17420206,
CC ECO:0000269|PubMed:19047379, ECO:0000269|PubMed:8226621}.
CC -!- PHARMACEUTICAL: May be a drug target for designing new drugs that kill
CC persister bacteria for more effective control of bacterial infections.
CC -!- SIMILARITY: Belongs to the PhoU family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be involved in phosphate transport.
CC {ECO:0000305|PubMed:1459954}.
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DR EMBL; X02723; CAA26510.1; -; Genomic_DNA.
DR EMBL; K01992; AAA24382.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62075.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76747.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77564.1; -; Genomic_DNA.
DR EMBL; M16487; AAA23507.1; -; Genomic_DNA.
DR PIR; D23311; BVECPU.
DR RefSeq; NP_418180.1; NC_000913.3.
DR RefSeq; WP_000377786.1; NZ_STEB01000015.1.
DR AlphaFoldDB; P0A9K7; -.
DR SMR; P0A9K7; -.
DR BioGRID; 4262141; 51.
DR DIP; DIP-10503N; -.
DR IntAct; P0A9K7; 1.
DR STRING; 511145.b3724; -.
DR jPOST; P0A9K7; -.
DR PaxDb; P0A9K7; -.
DR PRIDE; P0A9K7; -.
DR EnsemblBacteria; AAC76747; AAC76747; b3724.
DR EnsemblBacteria; BAE77564; BAE77564; BAE77564.
DR GeneID; 66672376; -.
DR GeneID; 948233; -.
DR KEGG; ecj:JW3702; -.
DR KEGG; eco:b3724; -.
DR PATRIC; fig|1411691.4.peg.2976; -.
DR EchoBASE; EB0728; -.
DR eggNOG; COG0704; Bacteria.
DR HOGENOM; CLU_078518_2_1_6; -.
DR InParanoid; P0A9K7; -.
DR OMA; WKHGIET; -.
DR PhylomeDB; P0A9K7; -.
DR BioCyc; EcoCyc:EG10735-MON; -.
DR PRO; PR:P0A9K7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; TAS:UniProtKB.
DR GO; GO:0071236; P:cellular response to antibiotic; IMP:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IMP:UniProtKB.
DR GO; GO:0071467; P:cellular response to pH; IMP:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0032413; P:negative regulation of ion transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0045936; P:negative regulation of phosphate metabolic process; IMP:UniProtKB.
DR GO; GO:2000186; P:negative regulation of phosphate transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR Gene3D; 1.20.58.220; -; 2.
DR InterPro; IPR028366; P_transport_PhoU.
DR InterPro; IPR038078; PhoU-like_sf.
DR InterPro; IPR026022; PhoU_dom.
DR PANTHER; PTHR42930; PTHR42930; 1.
DR Pfam; PF01895; PhoU; 2.
DR PIRSF; PIRSF003107; PhoU; 1.
DR TIGRFAMs; TIGR02135; phoU_full; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Pharmaceutical; Phosphate transport;
KW Reference proteome; Transport.
FT CHAIN 1..241
FT /note="Phosphate-specific transport system accessory
FT protein PhoU"
FT /id="PRO_0000155168"
SQ SEQUENCE 241 AA; 27417 MW; 29843C1C3827FACD CRC64;
MDSLNLNKHI SGQFNAELES IRTQVMTMGG MVEQQLSDAI TAMHNQDSDL AKRVIEGDKN
VNMMEVAIDE ACVRIIAKRQ PTASDLRLVM VISKTIAELE RIGDVADKIC RTALEKFSQQ
HQPLLVSLES LGRHTIQMLH DVLDAFARMD IDEAVRIYRE DKKVDQEYEG IVRQLMTYMM
EDSRTIPSVL TALFCARSIE RIGDRCQNIC EFIFYYVKGQ DFRHVGGDEL DKLLAGKDSD
K
