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P0AEJ4 (ENVZ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. 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:
Osmolarity sensor protein EnvZ

EC=2.7.13.3
Gene names
Name:envZ
Synonyms:ompB, perA, tpo
Ordered Locus Names:b3404, JW3367
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Enzyme regulation

Activity is modulated by MzrA. Ref.12 Ref.13

Subunit structure

Homodimer. Interacts with MzrA. Ref.10 Ref.12 Ref.13 Ref.15

Subcellular location

Cell inner membrane; Multi-pass membrane protein.

Domain

The HAMP domain by itself is intrinsically disordered. Ref.11

Post-translational modification

Autophosphorylated. Ref.5 Ref.14

Sequence similarities

Contains 1 HAMP domain.

Contains 1 histidine kinase domain.

Ontologies

Keywords
   Biological processTwo-component regulatory system
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to acid

Inferred from mutant phenotype PubMed 20380141. Source: EcoliWiki

detection of temperature stimulus

Inferred from genetic interaction Ref.12. Source: EcoliWiki

phosphorelay signal transduction system

Inferred from direct assay PubMed 2558046. Source: EcoliWiki

phosphorylation

Inferred from direct assay PubMed 2558046. Source: EcoliWiki

protein autophosphorylation

Inferred from mutant phenotype PubMed 10973966. Source: CACAO

protein dephosphorylation

Inferred from direct assay PubMed 2558046. Source: EcoliWiki

regulation of response to osmotic stress

Inferred from mutant phenotype PubMed 3536870. Source: EcoCyc

signal transduction by phosphorylation

Inferred from mutant phenotype PubMed 2668953. Source: GOC

   Cellular_componentcytoplasmic side of plasma membrane

Inferred from direct assay Ref.7. Source: EcoCyc

integral component of plasma membrane

Inferred from direct assay Ref.7. Source: EcoCyc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from direct assay PubMed 2558046. Source: EcoCyc

phosphorelay sensor kinase activity

Inferred from mutant phenotype PubMed 2668953. Source: EcoCyc

protein binding

Inferred from physical interaction Ref.12Ref.13. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mzrAP426153EBI-1121750,EBI-6412632

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Osmolarity sensor protein EnvZ
PRO_0000074759

Regions

Topological domain1 – 1515Cytoplasmic Probable
Transmembrane16 – 3520Helical; Probable
Topological domain36 – 158123Periplasmic Probable
Transmembrane159 – 17921Helical; Probable
Topological domain180 – 450271Cytoplasmic Probable
Domain180 – 23253HAMP
Domain240 – 440201Histidine kinase
Nucleotide binding373 – 38715ATP

Sites

Binding site3471ATP

Amino acid modifications

Modified residue2431Phosphohistidine; by autocatalysis Ref.5

Experimental info

Mutagenesis1931A → L: Promotes the formation of alpha-helical secondary structure of the HAMP domain. Ref.11
Mutagenesis1931A → V: No effect. Ref.11
Mutagenesis3471N → D: Loss of ATP binding; loss of autophosphorylation. Ref.14

Secondary structure

...................................... 450
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AEJ4 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: D58444D038722146

FASTA45050,334
        10         20         30         40         50         60 
MRRLRFSPRS SFARTLLLIV TLLFASLVTT YLVVLNFAIL PSLQQFNKVL AYEVRMLMTD 

        70         80         90        100        110        120 
KLQLEDGTQL VVPPAFRREI YRELGISLYS NEAAEEAGLR WAQHYEFLSH QMAQQLGGPT 

       130        140        150        160        170        180 
EVRVEVNKSS PVVWLKTWLS PNIWVRVPLT EIHQGDFSPL FRYTLAIMLL AIGGAWLFIR 

       190        200        210        220        230        240 
IQNRPLVDLE HAALQVGKGI IPPPLREYGA SEVRSVTRAF NHMAAGVKQL ADDRTLLMAG 

       250        260        270        280        290        300 
VSHDLRTPLT RIRLATEMMS EQDGYLAESI NKDIEECNAI IEQFIDYLRT GQEMPMEMAD 

       310        320        330        340        350        360 
LNAVLGEVIA AESGYEREIE TALYPGSIEV KMHPLSIKRA VANMVVNAAR YGNGWIKVSS 

       370        380        390        400        410        420 
GTEPNRAWFQ VEDDGPGIAP EQRKHLFQPF VRGDSARTIS GTGLGLAIVQ RIVDNHNGML 

       430        440        450 
ELGTSERGGL SIRAWLPVPV TRAQGTTKEG 

« Hide

References

« Hide 'large scale' references
[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]"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.
[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]"NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ."
Tanaka T., Saha S.K., Tomomori C., Ishima R., Liu D., Tong K.I., Park H., Dutta R., Qin L., Swindells M.B., Yamazaki T., Ono A.M., Kainosho M., Inouye M., Ikura M.
Nature 396:88-92(1998) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01656 Unassigned RNA. Translation: AAA16242.1.
U18997 Genomic DNA. Translation: AAA58201.1.
U00096 Genomic DNA. Translation: AAC76429.1.
AP009048 Genomic DNA. Translation: BAE77887.1.
PIRMMECZB. B25024.
RefSeqNP_417863.1. NC_000913.3.
YP_492028.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0AEJ4.
SMRP0AEJ4. Positions 184-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48357N.
IntActP0AEJ4. 5 interactions.
MINTMINT-8398485.
STRING511145.b3404.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76429; AAC76429; b3404.
BAE77887; BAE77887; BAE77887.
GeneID12932272.
947272.
KEGGecj:Y75_p3772.
eco:b3404.
PATRIC32122244. VBIEscCol129921_3499.

Organism-specific databases

EchoBASEEB0265.
EcoGeneEG10269. envZ.

Phylogenomic databases

eggNOGCOG0642.
HOGENOMHOG000218774.
KOK07638.
OMAQDRVEHE.
OrthoDBEOG6G4VQG.
PhylomeDBP0AEJ4.

Enzyme and pathway databases

BioCycEcoCyc:ENVZ-MONOMER.
ECOL316407:JW3367-MONOMER.

Gene expression databases

GenevestigatorP0AEJ4.

Family and domain databases

Gene3D1.10.287.130. 1 hit.
3.30.565.10. 1 hit.
InterProIPR003661. 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]
PfamPF00672. HAMP. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
[Graphical view]
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00304. HAMP. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
[Graphical view]
SUPFAMSSF47384. SSF47384. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEPS50885. HAMP. 1 hit.
PS50109. HIS_KIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AEJ4.
PROP0AEJ4.

Entry information

Entry nameENVZ_ECOLI
AccessionPrimary (citable) accession number: P0AEJ4
Secondary accession number(s): P02933, Q2M769
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 20, 2005
Last modified: July 9, 2014
This is version 86 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