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P23836

- PHOP_ECOLI

UniProt

P23836 - PHOP_ECOLI

Protein

Transcriptional regulatory protein PhoP

Gene

phoP

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    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

    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

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. phosphorelay response regulator activity Source: InterPro

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Two-component regulatory system

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PHOP-MONOMER.
    ECOL316407:JW1116-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10731. phoP.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 223223Transcriptional regulatory protein PhoPPRO_0000081195Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei51 – 5114-aspartylphosphatePROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylated by PhoQ.Curated

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP23836.
    PRIDEiP23836.

    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

    GenevestigatoriP23836.

    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

    Protein-protein interaction databases

    DIPiDIP-10500N.
    IntActiP23836. 5 interactions.
    STRINGi511145.b1130.

    Structurei

    Secondary structure

    1
    223
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Helixi10 – 2213
    Beta strandi26 – 327
    Helixi33 – 4210
    Beta strandi46 – 505
    Beta strandi55 – 573
    Helixi59 – 6810
    Beta strandi75 – 806
    Helixi84 – 929
    Beta strandi96 – 1027
    Helixi105 – 11915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PKXX-ray2.54A/B1-121[»]
    2PL1X-ray1.90A1-121[»]
    ProteinModelPortaliP23836.
    SMRiP23836. Positions 1-221.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23836.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 116116Response regulatoryPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 response regulatory domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0745.
    HOGENOMiHOG000034815.
    KOiK07660.
    OMAiVELPVIM.
    OrthoDBiEOG6G4VQG.
    PhylomeDBiP23836.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR011006. CheY-like_superfamily.
    IPR001867. Sig_transdc_resp-reg_C.
    IPR001789. Sig_transdc_resp-reg_receiver.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00072. Response_reg. 1 hit.
    PF00486. Trans_reg_C. 1 hit.
    [Graphical view]
    SMARTiSM00448. REC. 1 hit.
    SM00862. Trans_reg_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF52172. SSF52172. 1 hit.
    PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23836-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRVLVVEDNA LLRHHLKVQI QDAGHQVDDA EDAKEADYYL NEHIPDIAIV    50
    DLGLPDEDGL SLIRRWRSND VSLPILVLTA RESWQDKVEV LSAGADDYVT 100
    KPFHIEEVMA RMQALMRRNS GLASQVISLP PFQVDLSRRE LSINDEVIKL 150
    TAFEYTIMET LIRNNGKVVS KDSLMLQLYP DAELRESHTI DVLMGRLRKK 200
    IQAQYPQEVI TTVRGQGYLF ELR 223
    Length:223
    Mass (Da):25,535
    Last modified:November 1, 1991 - v1
    Checksum:i2EFF27E3923D43EF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_489398.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74214; AAC74214; b1130.
    BAA35952; BAA35952; BAA35952.
    GeneIDi12931100.
    945697.
    KEGGiecj:Y75_p1100.
    eco:b1130.
    PATRICi32117509. VBIEscCol129921_1177.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A41965.
    RefSeqi NP_415648.1. NC_000913.3.
    YP_489398.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PKX X-ray 2.54 A/B 1-121 [» ]
    2PL1 X-ray 1.90 A 1-121 [» ]
    ProteinModelPortali P23836.
    SMRi P23836. Positions 1-221.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10500N.
    IntActi P23836. 5 interactions.
    STRINGi 511145.b1130.

    Proteomic databases

    PaxDbi P23836.
    PRIDEi P23836.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74214 ; AAC74214 ; b1130 .
    BAA35952 ; BAA35952 ; BAA35952 .
    GeneIDi 12931100.
    945697.
    KEGGi ecj:Y75_p1100.
    eco:b1130.
    PATRICi 32117509. VBIEscCol129921_1177.

    Organism-specific databases

    EchoBASEi EB0724.
    EcoGenei EG10731. phoP.

    Phylogenomic databases

    eggNOGi COG0745.
    HOGENOMi HOG000034815.
    KOi K07660.
    OMAi VELPVIM.
    OrthoDBi EOG6G4VQG.
    PhylomeDBi P23836.

    Enzyme and pathway databases

    BioCyci EcoCyc:PHOP-MONOMER.
    ECOL316407:JW1116-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P23836.
    PROi P23836.

    Gene expression databases

    Genevestigatori P23836.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR011006. CheY-like_superfamily.
    IPR001867. Sig_transdc_resp-reg_C.
    IPR001789. Sig_transdc_resp-reg_receiver.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00072. Response_reg. 1 hit.
    PF00486. Trans_reg_C. 1 hit.
    [Graphical view ]
    SMARTi SM00448. REC. 1 hit.
    SM00862. Trans_reg_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52172. SSF52172. 1 hit.
    PROSITEi PS50110. RESPONSE_REGULATORY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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. "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.

    Entry informationi

    Entry nameiPHOP_ECOLI
    AccessioniPrimary (citable) accession number: P23836
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.

    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
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3