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Protein

Phosphate-specific transport system accessory protein PhoU

Gene

phoU

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • magnesium ion binding Source: EcoCyc
  • manganese ion binding Source: EcoCyc
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • cellular phosphate ion homeostasis Source: UniProtKB
  • cellular response to antibiotic Source: UniProtKB
  • cellular response to heat Source: UniProtKB
  • cellular response to pH Source: UniProtKB
  • cellular response to phosphate starvation Source: UniProtKB
  • cellular response to starvation Source: UniProtKB
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of ion transmembrane transporter activity Source: UniProtKB
  • negative regulation of phosphate metabolic process Source: UniProtKB
  • negative regulation of phosphate transmembrane transport Source: UniProtKB
  • pathogenesis Source: UniProtKB
  • phosphate ion transport Source: UniProtKB-KW
  • regulation of cell growth Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Phosphate transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG10735-MONOMER.
ECOL316407:JW3702-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphate-specific transport system accessory protein PhoU
Short name:
Pst system accessory protein PhoU
Alternative name(s):
Negative regulator of Pho regulon
Gene namesi
Name:phoU
Synonyms:nmpA
Ordered Locus Names:b3724, JW3702
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10735. phoU.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extrinsic component of plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Pharmaceutical usei

May be a drug target for designing new drugs that kill persister bacteria for more effective control of bacterial infections.

Disruption phenotypei

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).5 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Phosphate-specific transport system accessory protein PhoUPRO_0000155168Add
BLAST

Proteomic databases

PaxDbiP0A9K7.
PRIDEiP0A9K7.

Expressioni

Inductioni

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).2 Publications

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
glpDP130351EBI-1133614,EBI-548509

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4262141. 13 interactions.
DIPiDIP-10503N.
IntActiP0A9K7. 1 interaction.
STRINGi511145.b3724.

Structurei

3D structure databases

ProteinModelPortaliP0A9K7.
SMRiP0A9K7. Positions 11-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PhoU family.Curated

Phylogenomic databases

eggNOGiENOG4108UTW. Bacteria.
COG0704. LUCA.
HOGENOMiHOG000074025.
InParanoidiP0A9K7.
KOiK02039.
OMAiELATYMM.
OrthoDBiEOG6Q2SPF.
PhylomeDBiP0A9K7.

Family and domain databases

InterProiIPR028366. P_trasport_PhoU.
IPR026022. PhoU_dom.
[Graphical view]
PANTHERiPTHR10010:SF14. PTHR10010:SF14. 1 hit.
PfamiPF01895. PhoU. 2 hits.
[Graphical view]
PIRSFiPIRSF003107. PhoU. 1 hit.
TIGRFAMsiTIGR02135. phoU_full. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A9K7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSLNLNKHI SGQFNAELES IRTQVMTMGG MVEQQLSDAI TAMHNQDSDL
60 70 80 90 100
AKRVIEGDKN VNMMEVAIDE ACVRIIAKRQ PTASDLRLVM VISKTIAELE
110 120 130 140 150
RIGDVADKIC RTALEKFSQQ HQPLLVSLES LGRHTIQMLH DVLDAFARMD
160 170 180 190 200
IDEAVRIYRE DKKVDQEYEG IVRQLMTYMM EDSRTIPSVL TALFCARSIE
210 220 230 240
RIGDRCQNIC EFIFYYVKGQ DFRHVGGDEL DKLLAGKDSD K
Length:241
Mass (Da):27,417
Last modified:April 1, 1988 - v1
Checksum:i29843C1C3827FACD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02723 Genomic DNA. Translation: CAA26510.1.
K01992 Genomic DNA. Translation: AAA24382.1.
L10328 Genomic DNA. Translation: AAA62075.1.
U00096 Genomic DNA. Translation: AAC76747.1.
AP009048 Genomic DNA. Translation: BAE77564.1.
M16487 Genomic DNA. Translation: AAA23507.1.
PIRiD23311. BVECPU.
RefSeqiNP_418180.1. NC_000913.3.
WP_000377786.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76747; AAC76747; b3724.
BAE77564; BAE77564; BAE77564.
GeneIDi948233.
KEGGiecj:JW3702.
eco:b3724.
PATRICi32122945. VBIEscCol129921_3848.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02723 Genomic DNA. Translation: CAA26510.1.
K01992 Genomic DNA. Translation: AAA24382.1.
L10328 Genomic DNA. Translation: AAA62075.1.
U00096 Genomic DNA. Translation: AAC76747.1.
AP009048 Genomic DNA. Translation: BAE77564.1.
M16487 Genomic DNA. Translation: AAA23507.1.
PIRiD23311. BVECPU.
RefSeqiNP_418180.1. NC_000913.3.
WP_000377786.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0A9K7.
SMRiP0A9K7. Positions 11-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262141. 13 interactions.
DIPiDIP-10503N.
IntActiP0A9K7. 1 interaction.
STRINGi511145.b3724.

Proteomic databases

PaxDbiP0A9K7.
PRIDEiP0A9K7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76747; AAC76747; b3724.
BAE77564; BAE77564; BAE77564.
GeneIDi948233.
KEGGiecj:JW3702.
eco:b3724.
PATRICi32122945. VBIEscCol129921_3848.

Organism-specific databases

EchoBASEiEB0728.
EcoGeneiEG10735. phoU.

Phylogenomic databases

eggNOGiENOG4108UTW. Bacteria.
COG0704. LUCA.
HOGENOMiHOG000074025.
InParanoidiP0A9K7.
KOiK02039.
OMAiELATYMM.
OrthoDBiEOG6Q2SPF.
PhylomeDBiP0A9K7.

Enzyme and pathway databases

BioCyciEcoCyc:EG10735-MONOMER.
ECOL316407:JW3702-MONOMER.

Miscellaneous databases

PROiP0A9K7.

Family and domain databases

InterProiIPR028366. P_trasport_PhoU.
IPR026022. PhoU_dom.
[Graphical view]
PANTHERiPTHR10010:SF14. PTHR10010:SF14. 1 hit.
PfamiPF01895. PhoU. 2 hits.
[Graphical view]
PIRSFiPIRSF003107. PhoU. 1 hit.
TIGRFAMsiTIGR02135. phoU_full. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the genes involved in phosphate transport and regulation of the phosphate regulon in Escherichia coli."
    Amemura M., Makino K., Shinagawa H., Kobayashi A., Nakata A.
    J. Mol. Biol. 184:241-250(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships."
    Surin B.P., Rosenberg H., Cox G.B.
    J. Bacteriol. 161:189-198(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "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."
    Schnetz K., Toloczyki C., Rak B.
    J. Bacteriol. 169:2579-2590(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-241.
    Strain: K12.
  7. "Purification of the phoU protein, a negative regulator of the pho regulon of Escherichia coli K-12."
    Surin B.P., Dixon N.E., Rosenberg H.
    J. Bacteriol. 168:631-635(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-22, SUBCELLULAR LOCATION.
  8. "Regulation of the pho regulon in Escherichia coli K-12. Genetic and physiological regulation of the positive regulatory gene phoB."
    Shinagawa H., Makino K., Nakata A.
    J. Mol. Biol. 168:477-488(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS REPRESSOR OF PHO REGULON.
  9. "Regulation of the phosphate regulon in Escherichia coli K-12: regulation of the negative regulatory gene phoU and identification of the gene product."
    Nakata A., Amemura M., Shinagawa H.
    J. Bacteriol. 159:979-985(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUGGESTION OF FUNCTION AS A REPRESSOR OF PHOB, INDUCTION.
  10. "Role of PhoU in phosphate transport and alkaline phosphatase regulation."
    Muda M., Rao N.N., Torriani A.
    J. Bacteriol. 174:8057-8064(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: K12 / K10.
  11. "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."
    Steed P.M., Wanner B.L.
    J. Bacteriol. 175:6797-6809(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: K12.
  12. "Accumulation of inorganic polyphosphate in phoU mutants of Escherichia coli and Synechocystis sp. strain PCC6803."
    Morohoshi T., Maruo T., Shirai Y., Kato J., Ikeda T., Takiguchi N., Ohtake H., Kuroda A.
    Appl. Environ. Microbiol. 68:4107-4110(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: K12 / MG1655 / ATCC 47076.
  13. "Transcriptional analysis of the pst operon of Escherichia coli."
    Aguena M., Yagil E., Spira B.
    Mol. Genet. Genomics 268:518-524(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPT ANALYSIS, OPERON STRUCTURE.
    Strain: K12 / MG1655 / ATCC 47076.
  14. "PhoU is a persistence switch involved in persister formation and tolerance to multiple antibiotics and stresses in Escherichia coli."
    Li Y., Zhang Y.
    Antimicrob. Agents Chemother. 51:2092-2099(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TOLERANCE TO ANTIBIOTICS AND VARIOUS STRESSES, DISRUPTION PHENOTYPE, POTENTIAL DRUG TARGET.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  15. "Transcript and protein level analyses of the interactions among PhoB, PhoR, PhoU and CreC in response to phosphate starvation in Escherichia coli."
    Baek J.H., Kang Y.J., Lee S.Y.
    FEMS Microbiol. Lett. 277:254-259(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  16. "The phosphate regulon and bacterial virulence: a regulatory network connecting phosphate homeostasis and pathogenesis."
    Lamarche M.G., Wanner B.L., Crepin S., Harel J.
    FEMS Microbiol. Rev. 32:461-473(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  17. "Employment of a promoter-swapping technique shows that PhoU modulates the activity of the PstSCAB2 ABC transporter in Escherichia coli."
    Rice C.D., Pollard J.E., Lewis Z.T., McCleary W.R.
    Appl. Environ. Microbiol. 75:573-582(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, EFFECT OF MUTATIONS ON REPRESSION OF AP ACTIVITY.
  18. "Global regulation by the seven-component Pi signaling system."
    Hsieh Y.J., Wanner B.L.
    Curr. Opin. Microbiol. 13:198-203(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiPHOU_ECOLI
AccessioniPrimary (citable) accession number: P0A9K7
Secondary accession number(s): P07656, Q2M842
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: January 20, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be involved in phosphate transport.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.