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P23836 (PHOP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional regulatory protein PhoP
Gene names
Name:phoP
Ordered Locus Names:b1130, JW1116
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg2+ environments and the control of acid resistance genes. In low periplasmic Mg2+, PhoQ phosphorylates PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg2+, PhoQ dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG By similarity. Mediates magnesium influx to the cytosol by activation of MgtA. Promotes expression of the two-component regulatory system rstA/rstB and transcription of the hemL, mgrB, nagA, slyB, vboR and yrbL genes. Ref.10

Enzyme regulation

Feedback inhibited by MgrB, which seems to bind PhoQ, altering its activity and that of downstream effector PhoP. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, or treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Ref.15 Ref.16

Subunit structure

Monomer in the inactive, unphosphorylated state and dimer in the active, phosphorylated state Probable. Ref.17

Subcellular location

Cytoplasm Probable.

Induction

The phoP/phoQ operon is positively autoregulated by both PhoP and PhoQ in a Mg2+-dependent manner, inhibited at high Mg2+ concentrations (Ref.10). Induced by dsbA disruption and dithiothreitol (Ref.16). Ref.10 Ref.11 Ref.15 Ref.16

Post-translational modification

Phosphorylated by PhoQ Probable. Ref.17

Disruption phenotype

Altered expression of 33 genes; 9 are down-regulated, the rest up-regulated. Ref.14

Miscellaneous

There is a close linkage between the Rcs and PhoQ/P signaling systems, and both signaling systems respond to certain external divalent cations (zinc and magnesium).

Two-component regulatory system EvgA/EvgS interacts with PhoP/PhoQ via signal transduction mediated by phospho-EvgA.

Sequence similarities

Contains 1 response regulatory domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself5EBI-1121453,EBI-1121453

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 223223Transcriptional regulatory protein PhoP
PRO_0000081195

Regions

Domain1 – 116116Response regulatory

Amino acid modifications

Modified residue5114-aspartylphosphate By similarity

Secondary structure

...................... 223
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23836 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 2EFF27E3923D43EF

FASTA22325,535
        10         20         30         40         50         60 
MRVLVVEDNA LLRHHLKVQI QDAGHQVDDA EDAKEADYYL NEHIPDIAIV DLGLPDEDGL 

        70         80         90        100        110        120 
SLIRRWRSND VSLPILVLTA RESWQDKVEV LSAGADDYVT KPFHIEEVMA RMQALMRRNS 

       130        140        150        160        170        180 
GLASQVISLP PFQVDLSRRE LSINDEVIKL TAFEYTIMET LIRNNGKVVS KDSLMLQLYP 

       190        200        210        220 
DAELRESHTI DVLMGRLRKK IQAQYPQEVI TTVRGQGYLF ELR 

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of the Escherichia coli phoP-phoQ operon."
Kasahara M., Nakata A., Shinagawa H.
J. Bacteriol. 174:492-498(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Molecular genetic analysis of the Escherichia coli phoP locus."
Groisman E.A., Heffron F., Solomon F.
J. Bacteriol. 174:486-491(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Escherichia coli purB gene: cloning, nucleotide sequence, and regulation by purR."
He B., Smith J.M., Zalkin H.
J. Bacteriol. 174:130-136(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
Strain: K12.
[7]Green S.M., Drabble W.T.
Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
Strain: K12.
[8]"Novel mode of transcription regulation of divergently overlapping promoters by PhoP, the regulator of two-component system sensing external magnesium availability."
Yamamoto K., Ogasawara H., Fujita N., Utsumi R., Ishihama A.
Mol. Microbiol. 45:423-438(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-7 AND 119-125.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[10]"Molecular characterization of the PhoP-PhoQ two-component system in Escherichia coli K-12: identification of extracellular Mg2+-responsive promoters."
Kato A., Tanabe H., Utsumi R.
J. Bacteriol. 181:5516-5520(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY LOW MG(2+).
Strain: K12 / MC4100 / JA176.
[11]"Identification and molecular characterization of the Mg2+ stimulon of Escherichia coli."
Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T., Mori H., Ishihama A., Utsumi R.
J. Bacteriol. 185:3696-3702(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME-WIDE ANALYSIS, REGULATION BY MG(2+).
Strain: K12 / MC4100 / JA176.
[12]"Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB phosphorelay system in Escherichia coli."
Hagiwara D., Sugiura M., Oshima T., Mori H., Aiba H., Yamashino T., Mizuno T.
J. Bacteriol. 185:5735-5746(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME-WIDE ANALYSIS.
Strain: K12 / ST001.
[13]"Signal transduction cascade between EvgA/EvgS and PhoP/PhoQ two-component systems of Escherichia coli."
Eguchi Y., Okada T., Minagawa S., Oshima T., Mori H., Yamamoto K., Ishihama A., Utsumi R.
J. Bacteriol. 186:3006-3014(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EVGA/EVGS.
Strain: K12 / MC4100 / JA176.
[14]"Dissecting the PhoP regulatory network of Escherichia coli and Salmonella enterica."
Zwir I., Shin D., Kato A., Nishino K., Latifi T., Solomon F., Hare J.M., Huang H., Groisman E.A.
Proc. Natl. Acad. Sci. U.S.A. 102:2862-2867(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ANALYSIS OF PHOP REGULATORY NETWORK, DISRUPTION PHENOTYPE.
Strain: K12 / MG1655 / ATCC 47076.
[15]"Feedback inhibition in the PhoQ/PhoP signaling system by a membrane peptide."
Lippa A.M., Goulian M.
PLoS Genet. 5:E1000788-E1000788(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
Strain: K12 / MG1655 / ATCC 47076.
[16]"Perturbation of the oxidizing environment of the periplasm stimulates the PhoQ/PhoP system in Escherichia coli."
Lippa A.M., Goulian M.
J. Bacteriol. 194:1457-1463(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INDUCTION.
Strain: K12 / MG1655 / ATCC 47076.
[17]"Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride."
Bachhawat P., Stock A.M.
J. Bacteriol. 189:5987-5995(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-120 IN THE PRESENCE AND ABSENCE OF PHOSPHORYLATION ANALOG, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90393 Genomic DNA. Translation: BAA14390.1.
M81433 Genomic DNA. Translation: AAA24377.1.
U00096 Genomic DNA. Translation: AAC74214.1.
AP009048 Genomic DNA. Translation: BAA35952.1.
M74924 Genomic DNA. Translation: AAA92732.1.
X59307 Genomic DNA. Translation: CAA41997.1.
PIRA41965.
RefSeqNP_415648.1. NC_000913.3.
YP_489398.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PKXX-ray2.54A/B1-121[»]
2PL1X-ray1.90A1-121[»]
ProteinModelPortalP23836.
SMRP23836. Positions 1-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10500N.
IntActP23836. 5 interactions.
STRING511145.b1130.

Proteomic databases

PaxDbP23836.
PRIDEP23836.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74214; AAC74214; b1130.
BAA35952; BAA35952; BAA35952.
GeneID12931100.
945697.
KEGGecj:Y75_p1100.
eco:b1130.
PATRIC32117509. VBIEscCol129921_1177.

Organism-specific databases

EchoBASEEB0724.
EcoGeneEG10731. phoP.

Phylogenomic databases

eggNOGCOG0745.
HOGENOMHOG000034815.
KOK07660.
OMAVELPVIM.
OrthoDBEOG6G4VQG.
PhylomeDBP23836.

Enzyme and pathway databases

BioCycEcoCyc:PHOP-MONOMER.
ECOL316407:JW1116-MONOMER.

Gene expression databases

GenevestigatorP23836.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR011006. CheY-like_superfamily.
IPR001867. Sig_transdc_resp-reg_C.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00072. Response_reg. 1 hit.
PF00486. Trans_reg_C. 1 hit.
[Graphical view]
SMARTSM00448. REC. 1 hit.
SM00862. Trans_reg_C. 1 hit.
[Graphical view]
SUPFAMSSF52172. SSF52172. 1 hit.
PROSITEPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23836.
PROP23836.

Entry information

Entry namePHOP_ECOLI
AccessionPrimary (citable) accession number: P23836
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene