Osmolarity sensor protein EnvZ - Escherichia coli (strain K12)

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P0AEJ4 (ENVZ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Osmolarity sensor protein EnvZ
EC=2.7.13.3

Gene names

Name:	envZ
Synonyms:	ompB, perA, tpo
Ordered Locus Names:	b3404, JW3367

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Two-component regulatory system
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to acid Inferred from mutant phenotype PubMed 20380141. Source: EcoliWiki detection of temperature stimulus Inferred from genetic interaction Ref.12. Source: EcoliWiki protein autophosphorylation Inferred from direct assay PubMed 2558046. Source: EcoliWiki protein dephosphorylation Inferred from direct assay PubMed 2558046. Source: EcoliWiki regulation of response to osmotic stress Inferred from mutant phenotype PubMed 3536870. Source: EcoCyc
Cellular_component	integral to plasma membrane Inferred from direct assay Ref.7. Source: EcoCyc internal side of plasma membrane Inferred from direct assay Ref.7. Source: EcoCyc
Molecular_function	ATP 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mzrA	P42615	3	EBI-1121750,EBI-6412632

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 450

450

Osmolarity sensor protein EnvZ

PRO_0000074759

Regions

Topological domain

1 – 15

Cytoplasmic Probable

Transmembrane

16 – 35

Helical; Probable

Topological domain

36 – 158

123

Periplasmic Probable

Transmembrane

159 – 179

Helical; Probable

Topological domain

180 – 450

271

Cytoplasmic Probable

Domain

180 – 232

HAMP

Domain

240 – 440

201

Histidine kinase

Nucleotide binding

373 – 387

ATP

Sites

Binding site

347

ATP

Amino acid modifications

Modified residue

243

Phosphohistidine; by autocatalysis Ref.5

Experimental info

Mutagenesis

193

A → L: Promotes the formation of alpha-helical secondary structure of the HAMP domain. Ref.11

Mutagenesis

193

A → V: No effect. Ref.11

Mutagenesis

347

N → D: Loss of ATP binding; loss of autophosphorylation. Ref.14

Secondary structure

450

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AEJ4 [UniParc].

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

FASTA

450

50,334

        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' referencesShow '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 277:1453-1474(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.

PIR

MMECZB. B25024.

RefSeq

NP_417863.1. NC_000913.2.
YP_492028.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	228-288	[»]
3ZRV	X-ray	1.65	A/B	228-290	[»]
3ZRW	X-ray	2.25	A/B/C/D	228-290	[»]
3ZRX	X-ray	1.25	A/B	228-289	[»]

ProteinModelPortal

P0AEJ4.

SMR

P0AEJ4. Positions 184-450.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48357N.

IntAct

P0AEJ4. 5 interactions.

STRING

511145.b3404.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76429; AAC76429; b3404.
BAE77887; BAE77887; BAE77887.

GeneID

12932272.
947272.

KEGG

ecj:Y75_p3772.
eco:b3404.

PATRIC

32122244. VBIEscCol129921_3499.

Organism-specific databases

EchoBASE

EB0265.

EcoGene

EG10269. envZ.

Phylogenomic databases

eggNOG

COG0642.

HOGENOM

HOG000218774.

K07638.

OMA

KPSYQQI.

ProtClustDB

PRK09467.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0AEJ4.

Family and domain databases

Gene3D

1.10.287.130. 1 hit.
3.30.565.10. 1 hit.

InterPro

IPR003660. HAMP_linker_domain.
IPR003594. HATPase_ATP-bd.
IPR004358. Sig_transdc_His_kin-like_C.
IPR003661. Sig_transdc_His_kin_sub1_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
[Graphical view]

Pfam

PF00672. HAMP. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
[Graphical view]

PRINTS

PR00344. BCTRLSENSOR.

SMART

SM00304. HAMP. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF47384. His_kin_homodim. 1 hit.

PROSITE

PS50885. HAMP. 1 hit.
PS50109. HIS_KIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AEJ4.

Entry information

Entry name

ENVZ_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents