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Protein

Osmolarity sensor protein EnvZ

Gene

envZ

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

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

  • ATP binding Source: UniProtKB-KW
  • phosphoprotein phosphatase activity Source: EcoCyc
  • phosphorelay sensor kinase activity Source: EcoCyc

GO - Biological processi

  • detection of temperature stimulus Source: EcoliWiki
  • peptidyl-histidine phosphorylation Source: GO_Central
  • phosphorelay signal transduction system Source: EcoliWiki
  • phosphorylation Source: EcoliWiki
  • protein autophosphorylation Source: CACAO
  • protein dephosphorylation Source: EcoliWiki
  • regulation of response to osmotic stress Source: EcoCyc
  • signal transduction by protein phosphorylation Source: GOC
Complete GO annotation...

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.
BRENDAi2.7.13.3. 2026.

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10269. envZ.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515CytoplasmicCuratedAdd
BLAST
Transmembranei16 – 3520HelicalCuratedAdd
BLAST
Topological domaini36 – 158123PeriplasmicCuratedAdd
BLAST
Transmembranei159 – 17921HelicalCuratedAdd
BLAST
Topological domaini180 – 450271CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

  • cytoplasmic side of plasma membrane Source: EcoCyc
  • integral component of plasma membrane Source: EcoCyc
  • intracellular Source: GOC
Complete GO annotation...

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. 1 Publication
Mutagenesisi193 – 1931A → V: No effect. 1 Publication
Mutagenesisi347 – 3471N → D: Loss of ATP binding; loss of autophosphorylation. 1 Publication

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 autocatalysisPROSITE-ProRule annotation1 Publication

Post-translational modificationi

Autophosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

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 – 25729Combined sources
Helixi261 – 2633Combined sources
Helixi264 – 28724Combined sources
Turni290 – 2923Combined sources
Beta strandi297 – 2993Combined sources
Helixi301 – 3099Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi319 – 3224Combined sources
Beta strandi329 – 3324Combined sources
Helixi334 – 35017Combined sources
Beta strandi352 – 3543Combined sources
Beta strandi356 – 3594Combined sources
Beta strandi369 – 3735Combined sources
Beta strandi378 – 3803Combined sources
Helixi383 – 3864Combined sources
Helixi394 – 3974Combined sources
Helixi402 – 41514Combined sources
Beta strandi419 – 4224Combined sources
Turni426 – 4283Combined sources
Beta strandi431 – 4355Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
InParanoidiP0AEJ4.
KOiK07638.
OMAiWIRPPQA.
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_C.
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

        10         20         30         40         50
MRRLRFSPRS SFARTLLLIV TLLFASLVTT YLVVLNFAIL PSLQQFNKVL
60 70 80 90 100
AYEVRMLMTD KLQLEDGTQL VVPPAFRREI YRELGISLYS NEAAEEAGLR
110 120 130 140 150
WAQHYEFLSH QMAQQLGGPT EVRVEVNKSS PVVWLKTWLS PNIWVRVPLT
160 170 180 190 200
EIHQGDFSPL FRYTLAIMLL AIGGAWLFIR IQNRPLVDLE HAALQVGKGI
210 220 230 240 250
IPPPLREYGA SEVRSVTRAF NHMAAGVKQL ADDRTLLMAG VSHDLRTPLT
260 270 280 290 300
RIRLATEMMS EQDGYLAESI NKDIEECNAI IEQFIDYLRT GQEMPMEMAD
310 320 330 340 350
LNAVLGEVIA AESGYEREIE TALYPGSIEV KMHPLSIKRA VANMVVNAAR
360 370 380 390 400
YGNGWIKVSS GTEPNRAWFQ VEDDGPGIAP EQRKHLFQPF VRGDSARTIS
410 420 430 440 450
GTGLGLAIVQ RIVDNHNGML ELGTSERGGL SIRAWLPVPV TRAQGTTKEG
Length:450
Mass (Da):50,334
Last modified:December 20, 2005 - v1
Checksum:iD58444D038722146
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Genome annotation databases

EnsemblBacteriaiAAC76429; AAC76429; b3404.
BAE77887; BAE77887; BAE77887.
GeneIDi947272.
KEGGiecj:Y75_p3772.
eco:b3404.
PATRICi32122244. VBIEscCol129921_3499.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76429; AAC76429; b3404.
BAE77887; BAE77887; BAE77887.
GeneIDi947272.
KEGGiecj:Y75_p3772.
eco:b3404.
PATRICi32122244. VBIEscCol129921_3499.

Organism-specific databases

EchoBASEiEB0265.
EcoGeneiEG10269. envZ.

Phylogenomic databases

eggNOGiCOG0642.
HOGENOMiHOG000218774.
InParanoidiP0AEJ4.
KOiK07638.
OMAiWIRPPQA.
OrthoDBiEOG6G4VQG.
PhylomeDBiP0AEJ4.

Enzyme and pathway databases

BioCyciEcoCyc:ENVZ-MONOMER.
ECOL316407:JW3367-MONOMER.
BRENDAi2.7.13.3. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AEJ4.
PROiP0AEJ4.

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_C.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 96 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

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 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.