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P0AEJ4

- ENVZ_ECOLI

UniProt

P0AEJ4 - ENVZ_ECOLI

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Protein
Osmolarity sensor protein EnvZ
Gene
envZ, ompB, perA, tpo, b3404, JW3367
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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 – 38715ATP
Add
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 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
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.

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515Cytoplasmic Inferred
Add
BLAST
Transmembranei16 – 3520Helical; Inferred
Add
BLAST
Topological domaini36 – 158123Periplasmic Inferred
Add
BLAST
Transmembranei159 – 17921Helical; Inferred
Add
BLAST
Topological domaini180 – 450271Cytoplasmic Inferred
Add
BLAST

GO - Cellular componenti

  1. cytoplasmic side of plasma membrane Source: EcoCyc
  2. integral component of plasma membrane Source: EcoCyc
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 EnvZ
PRO_0000074759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei243 – 2431Phosphohistidine; by autocatalysis1 Publication

Post-translational modificationi

Autophosphorylated.2 Publications

Keywords - PTMi

Phosphoprotein

Expressioni

Gene expression databases

GenevestigatoriP0AEJ4.

Interactioni

Subunit structurei

Homodimer. Interacts with MzrA.4 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

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.

Miscellaneous databases

EvolutionaryTraceiP0AEJ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini180 – 23253HAMP
Add
BLAST
Domaini240 – 440201Histidine kinase
Add
BLAST

Domaini

The HAMP domain by itself is intrinsically disordered.1 Publication

Sequence similaritiesi

Contains 1 HAMP domain.

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

« 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: July 9, 2014
This is version 86 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

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