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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)DescriptionActionsGraphical viewLength
Binding sitei347ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi373 – 387ATPAdd BLAST15

GO - Molecular functioni

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

GO - Biological processi

  • phosphorelay signal transduction system Source: EcoliWiki
  • phosphorylation Source: EcoliWiki
  • protein autophosphorylation Source: EcoliWiki
  • protein dephosphorylation Source: EcoliWiki
  • regulation of response to osmotic stress Source: EcoCyc

Keywordsi

Molecular functionKinase, Transferase
Biological processTwo-component regulatory system
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ENVZ-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10269. envZ.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 15CytoplasmicCuratedAdd BLAST15
Transmembranei16 – 35HelicalCuratedAdd BLAST20
Topological domaini36 – 158PeriplasmicCuratedAdd BLAST123
Transmembranei159 – 179HelicalCuratedAdd BLAST21
Topological domaini180 – 450CytoplasmicCuratedAdd BLAST271

GO - Cellular componenti

  • cytoplasmic side of plasma membrane Source: EcoCyc
  • integral component of plasma membrane Source: EcoCyc
  • intracellular Source: GOC

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi193A → L: Promotes the formation of alpha-helical secondary structure of the HAMP domain. 1 Publication1
Mutagenesisi193A → V: No effect. 1 Publication1
Mutagenesisi347N → D: Loss of ATP binding; loss of autophosphorylation. 1 Publication1

Chemistry databases

DrugBankiDB04395. Phosphoaminophosphonic Acid-Adenylate Ester.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000747591 – 450Osmolarity sensor protein EnvZAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei243Phosphohistidine; by autocatalysisPROSITE-ProRule annotation1 Publication1

Post-translational modificationi

Autophosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0AEJ4.
PRIDEiP0AEJ4.

PTM databases

iPTMnetiP0AEJ4.

Interactioni

Subunit structurei

Homodimer. Interacts with MzrA.5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261266. 12 interactors.
DIPiDIP-48357N.
IntActiP0AEJ4. 5 interactors.
MINTiMINT-8398485.
STRINGi316385.ECDH10B_3579.

Structurei

Secondary structure

1450
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 57Combined sources15
Beta strandi60 – 63Combined sources4
Beta strandi69 – 71Combined sources3
Helixi74 – 84Combined sources11
Beta strandi87 – 90Combined sources4
Helixi91 – 97Combined sources7
Helixi99 – 101Combined sources3
Helixi106 – 116Combined sources11
Beta strandi120 – 125Combined sources6
Beta strandi132 – 137Combined sources6
Beta strandi143 – 148Combined sources6
Helixi229 – 257Combined sources29
Helixi261 – 263Combined sources3
Helixi264 – 287Combined sources24
Turni290 – 292Combined sources3
Beta strandi297 – 299Combined sources3
Helixi301 – 309Combined sources9
Beta strandi314 – 316Combined sources3
Beta strandi319 – 322Combined sources4
Beta strandi329 – 332Combined sources4
Helixi334 – 350Combined sources17
Beta strandi352 – 354Combined sources3
Beta strandi356 – 359Combined sources4
Beta strandi369 – 373Combined sources5
Beta strandi378 – 380Combined sources3
Helixi383 – 386Combined sources4
Helixi394 – 397Combined sources4
Helixi402 – 415Combined sources14
Beta strandi419 – 422Combined sources4
Turni426 – 428Combined sources3
Beta strandi431 – 435Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5B1NX-ray1.33A223-289[»]
5B1OX-ray2.30A/B223-289[»]
5XGAX-ray1.95A36-158[»]
ProteinModelPortaliP0AEJ4.
SMRiP0AEJ4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEJ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini180 – 232HAMPPROSITE-ProRule annotationAdd BLAST53
Domaini240 – 440Histidine kinasePROSITE-ProRule annotationAdd BLAST201

Domaini

The HAMP domain by itself is intrinsically disordered.1 Publication

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105E0F. Bacteria.
ENOG410XTWD. LUCA.
HOGENOMiHOG000218774.
InParanoidiP0AEJ4.
KOiK07638.
PhylomeDBiP0AEJ4.

Family and domain databases

CDDicd06225. HAMP. 1 hit.
cd00075. HATPase_c. 1 hit.
cd00082. HisKA. 1 hit.
Gene3Di3.30.565.10. 1 hit.
InterProiView protein in InterPro
IPR003660. HAMP_dom.
IPR003594. HATPase_C.
IPR036890. HATPase_C_sf.
IPR005467. His_kinase_dom.
IPR003661. HisK_dim/P.
IPR036097. HisK_dim/P_sf.
IPR004358. Sig_transdc_His_kin-like_C.
PfamiView protein in Pfam
PF00672. HAMP. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
PRINTSiPR00344. BCTRLSENSOR.
SMARTiView protein in SMART
SM00304. HAMP. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
SUPFAMiSSF47384. SSF47384. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiView protein in PROSITE
PS50885. HAMP. 1 hit.
PS50109. HIS_KIN. 1 hit.

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.
WP_001253696.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76429; AAC76429; b3404.
BAE77887; BAE77887; BAE77887.
GeneIDi947272.
KEGGiecj:JW3367.
eco:b3404.
PATRICifig|1411691.4.peg.3325.

Similar proteinsi

Entry informationi

Entry nameiENVZ_ECOLI
AccessioniPrimary (citable) accession number: P0AEJ4
Secondary accession number(s): P02933, Q2M769
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 20, 2005
Last modified: November 22, 2017
This is version 116 of the entry and version 1 of the sequence. See 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