Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0AEJ4

- ENVZ_ECOLI

UniProt

P0AEJ4 - ENVZ_ECOLI

Protein

Osmolarity sensor protein EnvZ

Gene

envZ

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Member of the two-component regulatory system EnvZ/OmpR involved in the regulation of osmoregulation (genes ompF and ompC). EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals.

    Catalytic activityi

    ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

    Enzyme regulationi

    Activity is modulated by MzrA.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei347 – 3471ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi373 – 38715ATPAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphoprotein phosphatase activity Source: EcoCyc
    3. phosphorelay sensor kinase activity Source: EcoCyc
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to acid chemical Source: EcoliWiki
    2. detection of temperature stimulus Source: EcoliWiki
    3. phosphorelay signal transduction system Source: EcoliWiki
    4. phosphorylation Source: EcoliWiki
    5. protein autophosphorylation Source: CACAO
    6. protein dephosphorylation Source: EcoliWiki
    7. regulation of response to osmotic stress Source: EcoCyc
    8. signal transduction by phosphorylation Source: GOC

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Two-component regulatory system

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:ENVZ-MONOMER.
    ECOL316407:JW3367-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Osmolarity sensor protein EnvZ (EC:2.7.13.3)
    Gene namesi
    Name:envZ
    Synonyms:ompB, perA, tpo
    Ordered Locus Names:b3404, JW3367
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10269. envZ.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic side of plasma membrane Source: EcoCyc
    2. integral component of plasma membrane Source: EcoCyc

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi193 – 1931A → L: Promotes the formation of alpha-helical secondary structure of the HAMP domain. 2 Publications
    Mutagenesisi193 – 1931A → V: No effect. 2 Publications
    Mutagenesisi347 – 3471N → D: Loss of ATP binding; loss of autophosphorylation. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 450450Osmolarity sensor protein EnvZPRO_0000074759Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei243 – 2431Phosphohistidine; by autocatalysis1 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    Autophosphorylated.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Gene expression databases

    GenevestigatoriP0AEJ4.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with MzrA.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    mzrAP426153EBI-1121750,EBI-6412632

    Protein-protein interaction databases

    DIPiDIP-48357N.
    IntActiP0AEJ4. 5 interactions.
    MINTiMINT-8398485.
    STRINGi511145.b3404.

    Structurei

    Secondary structure

    1
    450
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi229 – 25729
    Helixi261 – 2633
    Helixi264 – 28724
    Turni290 – 2923
    Beta strandi297 – 3004
    Helixi301 – 3099
    Beta strandi314 – 3163
    Beta strandi319 – 3224
    Beta strandi329 – 3324
    Helixi334 – 35017
    Beta strandi352 – 3543
    Beta strandi356 – 3594
    Beta strandi369 – 3735
    Helixi380 – 3823
    Helixi383 – 3864
    Helixi394 – 3974
    Helixi402 – 41514
    Beta strandi419 – 4224
    Turni426 – 4283
    Beta strandi431 – 4355

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BXDNMR-A290-450[»]
    1JOYNMR-A/B223-289[»]
    1NJVmodel-A/B223-450[»]
    3ZCCX-ray1.25A/B229-288[»]
    3ZRVX-ray1.65A/B229-290[»]
    3ZRWX-ray2.25A/C/D229-289[»]
    B231-289[»]
    3ZRXX-ray1.25A/B229-289[»]
    4CTIX-ray2.85A/B/C/D228-450[»]
    4KP4X-ray3.00A/B223-253[»]
    A/B266-450[»]
    ProteinModelPortaliP0AEJ4.
    SMRiP0AEJ4. Positions 184-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AEJ4.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1515CytoplasmicCuratedAdd
    BLAST
    Topological domaini36 – 158123PeriplasmicCuratedAdd
    BLAST
    Topological domaini180 – 450271CytoplasmicCuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei16 – 3520HelicalCuratedAdd
    BLAST
    Transmembranei159 – 17921HelicalCuratedAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini180 – 23253HAMPPROSITE-ProRule annotationAdd
    BLAST
    Domaini240 – 440201Histidine kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The HAMP domain by itself is intrinsically disordered.1 Publication

    Sequence similaritiesi

    Contains 1 HAMP domain.PROSITE-ProRule annotation
    Contains 1 histidine kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0642.
    HOGENOMiHOG000218774.
    KOiK07638.
    OMAiQDRVEHE.
    OrthoDBiEOG6G4VQG.
    PhylomeDBiP0AEJ4.

    Family and domain databases

    Gene3Di1.10.287.130. 1 hit.
    3.30.565.10. 1 hit.
    InterProiIPR003661. EnvZ-like_dim/P.
    IPR003660. HAMP_linker_domain.
    IPR003594. HATPase_ATP-bd.
    IPR004358. Sig_transdc_His_kin-like_C.
    IPR005467. Sig_transdc_His_kinase_core.
    IPR009082. Sig_transdc_His_kinase_dimeric.
    [Graphical view]
    PfamiPF00672. HAMP. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF00512. HisKA. 1 hit.
    [Graphical view]
    PRINTSiPR00344. BCTRLSENSOR.
    SMARTiSM00304. HAMP. 1 hit.
    SM00387. HATPase_c. 1 hit.
    SM00388. HisKA. 1 hit.
    [Graphical view]
    SUPFAMiSSF47384. SSF47384. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEiPS50885. HAMP. 1 hit.
    PS50109. HIS_KIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0AEJ4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRLRFSPRS SFARTLLLIV TLLFASLVTT YLVVLNFAIL PSLQQFNKVL    50
    AYEVRMLMTD KLQLEDGTQL VVPPAFRREI YRELGISLYS NEAAEEAGLR 100
    WAQHYEFLSH QMAQQLGGPT EVRVEVNKSS PVVWLKTWLS PNIWVRVPLT 150
    EIHQGDFSPL FRYTLAIMLL AIGGAWLFIR IQNRPLVDLE HAALQVGKGI 200
    IPPPLREYGA SEVRSVTRAF NHMAAGVKQL ADDRTLLMAG VSHDLRTPLT 250
    RIRLATEMMS EQDGYLAESI NKDIEECNAI IEQFIDYLRT GQEMPMEMAD 300
    LNAVLGEVIA AESGYEREIE TALYPGSIEV KMHPLSIKRA VANMVVNAAR 350
    YGNGWIKVSS GTEPNRAWFQ VEDDGPGIAP EQRKHLFQPF VRGDSARTIS 400
    GTGLGLAIVQ RIVDNHNGML ELGTSERGGL SIRAWLPVPV TRAQGTTKEG 450
    Length:450
    Mass (Da):50,334
    Last modified:December 20, 2005 - v1
    Checksum:iD58444D038722146
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01656 Unassigned RNA. Translation: AAA16242.1.
    U18997 Genomic DNA. Translation: AAA58201.1.
    U00096 Genomic DNA. Translation: AAC76429.1.
    AP009048 Genomic DNA. Translation: BAE77887.1.
    PIRiB25024. MMECZB.
    RefSeqiNP_417863.1. NC_000913.3.
    YP_492028.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76429; AAC76429; b3404.
    BAE77887; BAE77887; BAE77887.
    GeneIDi12932272.
    947272.
    KEGGiecj:Y75_p3772.
    eco:b3404.
    PATRICi32122244. VBIEscCol129921_3499.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01656 Unassigned RNA. Translation: AAA16242.1 .
    U18997 Genomic DNA. Translation: AAA58201.1 .
    U00096 Genomic DNA. Translation: AAC76429.1 .
    AP009048 Genomic DNA. Translation: BAE77887.1 .
    PIRi B25024. MMECZB.
    RefSeqi NP_417863.1. NC_000913.3.
    YP_492028.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BXD NMR - A 290-450 [» ]
    1JOY NMR - A/B 223-289 [» ]
    1NJV model - A/B 223-450 [» ]
    3ZCC X-ray 1.25 A/B 229-288 [» ]
    3ZRV X-ray 1.65 A/B 229-290 [» ]
    3ZRW X-ray 2.25 A/C/D 229-289 [» ]
    B 231-289 [» ]
    3ZRX X-ray 1.25 A/B 229-289 [» ]
    4CTI X-ray 2.85 A/B/C/D 228-450 [» ]
    4KP4 X-ray 3.00 A/B 223-253 [» ]
    A/B 266-450 [» ]
    ProteinModelPortali P0AEJ4.
    SMRi P0AEJ4. Positions 184-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48357N.
    IntActi P0AEJ4. 5 interactions.
    MINTi MINT-8398485.
    STRINGi 511145.b3404.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76429 ; AAC76429 ; b3404 .
    BAE77887 ; BAE77887 ; BAE77887 .
    GeneIDi 12932272.
    947272.
    KEGGi ecj:Y75_p3772.
    eco:b3404.
    PATRICi 32122244. VBIEscCol129921_3499.

    Organism-specific databases

    EchoBASEi EB0265.
    EcoGenei EG10269. envZ.

    Phylogenomic databases

    eggNOGi COG0642.
    HOGENOMi HOG000218774.
    KOi K07638.
    OMAi QDRVEHE.
    OrthoDBi EOG6G4VQG.
    PhylomeDBi P0AEJ4.

    Enzyme and pathway databases

    BioCyci EcoCyc:ENVZ-MONOMER.
    ECOL316407:JW3367-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AEJ4.
    PROi P0AEJ4.

    Gene expression databases

    Genevestigatori P0AEJ4.

    Family and domain databases

    Gene3Di 1.10.287.130. 1 hit.
    3.30.565.10. 1 hit.
    InterProi IPR003661. EnvZ-like_dim/P.
    IPR003660. HAMP_linker_domain.
    IPR003594. HATPase_ATP-bd.
    IPR004358. Sig_transdc_His_kin-like_C.
    IPR005467. Sig_transdc_His_kinase_core.
    IPR009082. Sig_transdc_His_kinase_dimeric.
    [Graphical view ]
    Pfami PF00672. HAMP. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF00512. HisKA. 1 hit.
    [Graphical view ]
    PRINTSi PR00344. BCTRLSENSOR.
    SMARTi SM00304. HAMP. 1 hit.
    SM00387. HATPase_c. 1 hit.
    SM00388. HisKA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47384. SSF47384. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEi PS50885. HAMP. 1 hit.
    PS50109. HIS_KIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Osmoregulation of gene expression. II. DNA sequence of the envZ gene of the ompB operon of Escherichia coli and characterization of its gene product."
      Mizuno T., Wurtzel E.T., Inouye M.
      J. Biol. Chem. 257:13692-13698(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Primary characterization of the protein products of the Escherichia coli ompB locus: structure and regulation of synthesis of the OmpR and EnvZ proteins."
      Comeau D.E., Ikenaka K., Tsung K., Inouye M.
      J. Bacteriol. 164:578-584(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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.
    5. "Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli."
      Roberts D.L., Bennett D.W., Forst S.A.
      J. Biol. Chem. 269:8728-8733(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT HIS-243.
    6. "Transmembrane signal transduction and osmoregulation in Escherichia coli: I. Analysis by site-directed mutagenesis of the amino acid residues involved in phosphotransfer between the two regulatory components, EnvZ and OmpR."
      Kanamaru K., Aiba H., Mizuno T.
      J. Biochem. 108:483-487(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    7. "Localization and membrane topology of EnvZ, a protein involved in osmoregulation of OmpF and OmpC in Escherichia coli."
      Forst S., Comeau D., Norioka S., Inouye M.
      J. Biol. Chem. 262:16433-16438(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    8. "Transmembrane signal transduction and osmoregulation in Escherichia coli: functional importance of the transmembrane regions of membrane-located protein kinase, EnvZ."
      Tokishita S., Kojima A., Mizuno T.
      J. Biochem. 111:707-713(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "Global topology analysis of the Escherichia coli inner membrane proteome."
      Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
      Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
      Strain: K12 / MG1655 / ATCC 47076.
    10. "Structural characterization of Escherichia coli sensor histidine kinase EnvZ: the periplasmic C-terminal core domain is critical for homodimerization."
      Khorchid A., Inouye M., Ikura M.
      Biochem. J. 385:255-264(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    11. "Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli."
      Kishii R., Falzon L., Yoshida T., Kobayashi H., Inouye M.
      J. Biol. Chem. 282:26401-26408(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, MUTAGENESIS OF ALA-193.
    12. "MzrA: a novel modulator of the EnvZ/OmpR two-component regulon."
      Gerken H., Charlson E.S., Cicirelli E.M., Kenney L.J., Misra R.
      Mol. Microbiol. 72:1408-1422(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MZRA, ENZYME REGULATION.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    13. "MzrA-EnvZ interactions in the periplasm influence the EnvZ/OmpR two-component regulon."
      Gerken H., Misra R.
      J. Bacteriol. 192:6271-6278(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MZRA, ENZYME REGULATION.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    14. Cited for: STRUCTURE BY NMR OF 290-450 IN COMPLEX WITH ATP ANALOG, MUTAGENESIS OF ASN-347, AUTOPHOSPHORYLATION.
    15. "Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ."
      Tomomori C., Tanaka T., Dutta R., Park H., Saha S.K., Zhu Y., Ishima R., Liu D., Tong K.I., Kurokawa H., Qian H., Inouye M., Ikura M.
      Nat. Struct. Biol. 6:729-734(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 223-289, SUBUNIT.
    16. "Probing catalytically essential domain orientation in histidine kinase EnvZ by targeted disulfide crosslinking."
      Cai S./J., Khorchid A., Ikura M., Inouye M.
      J. Mol. Biol. 328:409-418(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 223-450, TOPOLOGY.

    Entry informationi

    Entry nameiENVZ_ECOLI
    AccessioniPrimary (citable) accession number: P0AEJ4
    Secondary accession number(s): P02933, Q2M769
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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