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Protein

Transcriptional regulatory protein PhoP

Gene

phoP

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

Functioni

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.By similarity1 Publication

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.

Enzyme regulationi

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.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi124 – 222OmpR/PhoB-typePROSITE-ProRule annotationAdd BLAST99

GO - Molecular functioni

  • bacterial-type RNA polymerase transcriptional activator activity, sequence-specific DNA binding Source: CollecTF
  • identical protein binding Source: IntAct
  • transcription regulatory region sequence-specific DNA binding Source: CollecTF

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation, Two-component regulatory system

Enzyme and pathway databases

BioCyciEcoCyc:PHOP-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulatory protein PhoP
Gene namesi
Name:phoP
Ordered Locus Names:b1130, JW1116
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10731 phoP

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • protein-DNA complex Source: CollecTF

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Altered expression of 33 genes; 9 are down-regulated, the rest up-regulated.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000811951 – 223Transcriptional regulatory protein PhoPAdd BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei514-aspartylphosphatePROSITE-ProRule annotation1

Post-translational modificationi

Phosphorylated by PhoQ.Curated

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP23836
PaxDbiP23836
PRIDEiP23836

PTM databases

iPTMnetiP23836

Expressioni

Inductioni

The phoP/phoQ operon is positively autoregulated by both PhoP and PhoQ in a Mg2+-dependent manner, inhibited at high Mg2+ concentrations (PubMed:10464230). Induced by dsbA disruption and dithiothreitol (PubMed:22267510).2 Publications

Gene expression databases

CollecTFiEXPREG_00000950

Interactioni

Subunit structurei

Monomer in the inactive, unphosphorylated state and dimer in the active, phosphorylated state.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-1121453,EBI-1121453

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4260094, 19 interactors
DIPiDIP-10500N
IntActiP23836, 6 interactors
STRINGi316385.ECDH10B_1202

Structurei

Secondary structure

1223
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi10 – 22Combined sources13
Beta strandi26 – 32Combined sources7
Helixi33 – 42Combined sources10
Beta strandi46 – 50Combined sources5
Beta strandi55 – 57Combined sources3
Helixi59 – 68Combined sources10
Beta strandi75 – 80Combined sources6
Helixi84 – 92Combined sources9
Beta strandi96 – 102Combined sources7
Helixi105 – 119Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PKXX-ray2.54A/B1-121[»]
2PL1X-ray1.90A1-121[»]
ProteinModelPortaliP23836
SMRiP23836
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23836

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 116Response regulatoryPROSITE-ProRule annotationAdd BLAST115

Phylogenomic databases

eggNOGiENOG4105XJC Bacteria
ENOG4111FPD LUCA
HOGENOMiHOG000034815
InParanoidiP23836
KOiK07660
OMAiDMVMSMQ
PhylomeDBiP23836

Family and domain databases

CDDicd00156 REC, 1 hit
cd00383 trans_reg_C, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR011006 CheY-like_superfamily
IPR001867 OmpR/PhoB-type_DNA-bd
IPR001789 Sig_transdc_resp-reg_receiver
IPR036388 WH-like_DNA-bd_sf
PfamiView protein in Pfam
PF00072 Response_reg, 1 hit
PF00486 Trans_reg_C, 1 hit
SMARTiView protein in SMART
SM00448 REC, 1 hit
SM00862 Trans_reg_C, 1 hit
SUPFAMiSSF52172 SSF52172, 1 hit
PROSITEiView protein in PROSITE
PS51755 OMPR_PHOB, 1 hit
PS50110 RESPONSE_REGULATORY, 1 hit

Sequencei

Sequence statusi: Complete.

P23836-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLVVEDNA LLRHHLKVQI QDAGHQVDDA EDAKEADYYL NEHIPDIAIV
60 70 80 90 100
DLGLPDEDGL SLIRRWRSND VSLPILVLTA RESWQDKVEV LSAGADDYVT
110 120 130 140 150
KPFHIEEVMA RMQALMRRNS GLASQVISLP PFQVDLSRRE LSINDEVIKL
160 170 180 190 200
TAFEYTIMET LIRNNGKVVS KDSLMLQLYP DAELRESHTI DVLMGRLRKK
210 220
IQAQYPQEVI TTVRGQGYLF ELR
Length:223
Mass (Da):25,535
Last modified:November 1, 1991 - v1
Checksum:i2EFF27E3923D43EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiA41965
RefSeqiNP_415648.1, NC_000913.3
WP_001265471.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74214; AAC74214; b1130
BAA35952; BAA35952; BAA35952
GeneIDi945697
KEGGiecj:JW1116
eco:b1130
PATRICifig|1411691.4.peg.1136

Similar proteinsi

Entry informationi

Entry nameiPHOP_ECOLI
AccessioniPrimary (citable) accession number: P23836
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 25, 2018
This is version 153 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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