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Phosphate-specific transport system accessory protein PhoU (Pst system accessory protein PhoU) (Negative regulator of Pho regulon)

 PHOU_ECOLI              Reviewed;         241 AA.
P0A9K7; P07656; Q2M842;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
07-NOV-2018, entry version 97.
RecName: Full=Phosphate-specific transport system accessory protein PhoU;
Short=Pst system accessory protein PhoU;
AltName: Full=Negative regulator of Pho regulon;
Name=phoU; Synonyms=nmpA; OrderedLocusNames=b3724, JW3702;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2993631; DOI=10.1016/0022-2836(85)90377-8;
Amemura M., Makino K., Shinagawa H., Kobayashi A., Nakata A.;
"Nucleotide sequence of the genes involved in phosphate transport and
regulation of the phosphate regulon in Escherichia coli.";
J. Mol. Biol. 184:241-250(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3881386;
Surin B.P., Rosenberg H., Cox G.B.;
"Phosphate-specific transport system of Escherichia coli: nucleotide
sequence and gene-polypeptide relationships.";
J. Bacteriol. 161:189-198(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7686882; DOI=10.1006/geno.1993.1230;
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
"DNA sequence and analysis of 136 kilobases of the Escherichia coli
genome: organizational symmetry around the origin of replication.";
Genomics 16:551-561(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-241.
STRAIN=K12;
PubMed=3034860; DOI=10.1128/jb.169.6.2579-2590.1987;
Schnetz K., Toloczyki C., Rak B.;
"Beta-glucoside (bgl) operon of Escherichia coli K-12: nucleotide
sequence, genetic organization, and possible evolutionary relationship
to regulatory components of two Bacillus subtilis genes.";
J. Bacteriol. 169:2579-2590(1987).
[7]
PROTEIN SEQUENCE OF 1-22, AND SUBCELLULAR LOCATION.
PubMed=3536855;
Surin B.P., Dixon N.E., Rosenberg H.;
"Purification of the phoU protein, a negative regulator of the pho
regulon of Escherichia coli K-12.";
J. Bacteriol. 168:631-635(1986).
[8]
FUNCTION AS REPRESSOR OF PHO REGULON.
PubMed=6310121; DOI=10.1016/S0022-2836(83)80297-6;
Shinagawa H., Makino K., Nakata A.;
"Regulation of the pho regulon in Escherichia coli K-12. Genetic and
physiological regulation of the positive regulatory gene phoB.";
J. Mol. Biol. 168:477-488(1983).
[9]
SUGGESTION OF FUNCTION AS A REPRESSOR OF PHOB, AND INDUCTION.
PubMed=6090402;
Nakata A., Amemura M., Shinagawa H.;
"Regulation of the phosphate regulon in Escherichia coli K-12:
regulation of the negative regulatory gene phoU and identification of
the gene product.";
J. Bacteriol. 159:979-985(1984).
[10]
DISRUPTION PHENOTYPE.
STRAIN=K12 / K10;
PubMed=1459954; DOI=10.1128/jb.174.24.8057-8064.1992;
Muda M., Rao N.N., Torriani A.;
"Role of PhoU in phosphate transport and alkaline phosphatase
regulation.";
J. Bacteriol. 174:8057-8064(1992).
[11]
DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=8226621; DOI=10.1128/jb.175.21.6797-6809.1993;
Steed P.M., Wanner B.L.;
"Use of the rep technique for allele replacement to construct mutants
with deletions of the pstSCAB-phoU operon: evidence of a new role for
the PhoU protein in the phosphate regulon.";
J. Bacteriol. 175:6797-6809(1993).
[12]
DISRUPTION PHENOTYPE.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=12147514; DOI=10.1128/AEM.68.8.4107-4110.2002;
Morohoshi T., Maruo T., Shirai Y., Kato J., Ikeda T., Takiguchi N.,
Ohtake H., Kuroda A.;
"Accumulation of inorganic polyphosphate in phoU mutants of
Escherichia coli and Synechocystis sp. strain PCC6803.";
Appl. Environ. Microbiol. 68:4107-4110(2002).
[13]
TRANSCRIPT ANALYSIS, AND OPERON STRUCTURE.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=12471449; DOI=10.1007/s00438-002-0764-4;
Aguena M., Yagil E., Spira B.;
"Transcriptional analysis of the pst operon of Escherichia coli.";
Mol. Genet. Genomics 268:518-524(2002).
[14]
FUNCTION IN TOLERANCE TO ANTIBIOTICS AND VARIOUS STRESSES, DISRUPTION
PHENOTYPE, AND POTENTIAL DRUG TARGET.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=17420206; DOI=10.1128/AAC.00052-07;
Li Y., Zhang Y.;
"PhoU is a persistence switch involved in persister formation and
tolerance to multiple antibiotics and stresses in Escherichia coli.";
Antimicrob. Agents Chemother. 51:2092-2099(2007).
[15]
INDUCTION.
PubMed=18031348; DOI=10.1111/j.1574-6968.2007.00965.x;
Baek J.H., Kang Y.J., Lee S.Y.;
"Transcript and protein level analyses of the interactions among PhoB,
PhoR, PhoU and CreC in response to phosphate starvation in Escherichia
coli.";
FEMS Microbiol. Lett. 277:254-259(2007).
[16]
REVIEW.
PubMed=18248418; DOI=10.1111/j.1574-6976.2008.00101.x;
Lamarche M.G., Wanner B.L., Crepin S., Harel J.;
"The phosphate regulon and bacterial virulence: a regulatory network
connecting phosphate homeostasis and pathogenesis.";
FEMS Microbiol. Rev. 32:461-473(2008).
[17]
DISRUPTION PHENOTYPE, AND EFFECT OF MUTATIONS ON REPRESSION OF AP
ACTIVITY.
PubMed=19047379; DOI=10.1128/AEM.01046-08;
Rice C.D., Pollard J.E., Lewis Z.T., McCleary W.R.;
"Employment of a promoter-swapping technique shows that PhoU modulates
the activity of the PstSCAB2 ABC transporter in Escherichia coli.";
Appl. Environ. Microbiol. 75:573-582(2009).
[18]
REVIEW.
PubMed=20171928; DOI=10.1016/j.mib.2010.01.014;
Hsieh Y.J., Wanner B.L.;
"Global regulation by the seven-component Pi signaling system.";
Curr. Opin. Microbiol. 13:198-203(2010).
-!- FUNCTION: Part of the phosphate (Pho) regulon, which plays a key
role in phosphate homeostasis. Encoded together with proteins of
the phosphate-specific transport (Pst) system in the polycistronic
pstSCAB-phoU operon. PhoU is essential for the repression of the
Pho regulon at high phosphate conditions. In this role, it may
bind, possibly as a chaperone, to PhoR, PhoB or a PhoR-PhoB
complex to promote dephosphorylation of phospho-PhoB, or inhibit
formation of the PhoR-PhoB transitory complex. Is also part of
complex networks important for bacterial virulence, tolerance to
antibiotics and stress response. {ECO:0000269|PubMed:17420206,
ECO:0000269|PubMed:6310121}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3536855}.
-!- INDUCTION: Expressed at higher levels under excess phosphate
culture conditions (PubMed:6090402). Induced by phosphate
starvation via the PhoR/PhoB two-component regulatory system
(PubMed:18031348). {ECO:0000269|PubMed:18031348,
ECO:0000269|PubMed:6090402}.
-!- DISRUPTION PHENOTYPE: Produces high level of alkaline phosphatase
(AP) when grown with excess phosphate (PubMed:1459954). No effect
on phosphate uptake, but particular deletion mutants have a severe
growth defect, which is largely alleviated by a compensatory
mutation in the pstSCAB genes or in the phoRB operon
(PubMed:8226621). Accumulates high levels of polyP, approximately
400 nmol of phosphate residues/mg of protein (PubMed:12147514).
Higher susceptibility to a diverse range of antibiotics including
ampicillin, norfloxacin and gentamicin, and stresses such as
starvation, acid pH, heat, peroxide, weak acids and energy
inhibitors, especially in stationary phase (PubMed:17420206).
Metabolically hyperactive status of the cell showing increased
expression of energy production genes, flagella and chemotaxis
genes, and a defect in persister formation (PubMed:17420206).
Cells transport phosphate via PstSCAB transporter system at
approximately 20% higher rate and accumulate higher levels of the
transporter and about 50% more phosphate in 12 minutes than wild-
type cells in phosphate-replete medium (PubMed:19047379).
{ECO:0000269|PubMed:12147514, ECO:0000269|PubMed:1459954,
ECO:0000269|PubMed:17420206, ECO:0000269|PubMed:19047379,
ECO:0000269|PubMed:8226621}.
-!- PHARMACEUTICAL: May be a drug target for designing new drugs that
kill persister bacteria for more effective control of bacterial
infections.
-!- SIMILARITY: Belongs to the PhoU family. {ECO:0000305}.
-!- CAUTION: Was originally thought to be involved in phosphate
transport. {ECO:0000305|PubMed:1459954}.
-----------------------------------------------------------------------
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EMBL; X02723; CAA26510.1; -; Genomic_DNA.
EMBL; K01992; AAA24382.1; -; Genomic_DNA.
EMBL; L10328; AAA62075.1; -; Genomic_DNA.
EMBL; U00096; AAC76747.1; -; Genomic_DNA.
EMBL; AP009048; BAE77564.1; -; Genomic_DNA.
EMBL; M16487; AAA23507.1; -; Genomic_DNA.
PIR; D23311; BVECPU.
RefSeq; NP_418180.1; NC_000913.3.
RefSeq; WP_000377786.1; NZ_LN832404.1.
ProteinModelPortal; P0A9K7; -.
SMR; P0A9K7; -.
BioGrid; 4262141; 51.
DIP; DIP-10503N; -.
IntAct; P0A9K7; 1.
STRING; 316385.ECDH10B_3911; -.
PaxDb; P0A9K7; -.
PRIDE; P0A9K7; -.
EnsemblBacteria; AAC76747; AAC76747; b3724.
EnsemblBacteria; BAE77564; BAE77564; BAE77564.
GeneID; 948233; -.
KEGG; ecj:JW3702; -.
KEGG; eco:b3724; -.
PATRIC; fig|1411691.4.peg.2976; -.
EchoBASE; EB0728; -.
EcoGene; EG10735; phoU.
eggNOG; ENOG4108UTW; Bacteria.
eggNOG; COG0704; LUCA.
HOGENOM; HOG000074025; -.
InParanoid; P0A9K7; -.
KO; K02039; -.
PhylomeDB; P0A9K7; -.
BioCyc; EcoCyc:EG10735-MONOMER; -.
PRO; PR:P0A9K7; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:EcoCyc.
GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0030643; P:cellular phosphate ion homeostasis; TAS:UniProtKB.
GO; GO:0071236; P:cellular response to antibiotic; IMP:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IMP:UniProtKB.
GO; GO:0071467; P:cellular response to pH; IMP:UniProtKB.
GO; GO:0016036; P:cellular response to phosphate starvation; IEP:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0032413; P:negative regulation of ion transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0045936; P:negative regulation of phosphate metabolic process; IMP:UniProtKB.
GO; GO:2000186; P:negative regulation of phosphate transmembrane transport; IMP:UniProtKB.
GO; GO:0009405; P:pathogenesis; IMP:UniProtKB.
GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
Gene3D; 1.20.58.220; -; 2.
InterPro; IPR028366; P_transport_PhoU.
InterPro; IPR038078; PhoU-like_sf.
InterPro; IPR026022; PhoU_dom.
PANTHER; PTHR42930:SF3; PTHR42930:SF3; 1.
Pfam; PF01895; PhoU; 2.
PIRSF; PIRSF003107; PhoU; 1.
TIGRFAMs; TIGR02135; phoU_full; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing;
Pharmaceutical; Phosphate transport; Reference proteome; Transport.
CHAIN 1 241 Phosphate-specific transport system
accessory protein PhoU.
/FTId=PRO_0000155168.
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


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