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ECOLI:ENVZ

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) envZ (synonyms: ompB, perA, tpo)
Protein Name(s) Osmolarity sensor protein EnvZ
External Links
UniProt P0AEJ4
EMBL J01656
U18997
U00096
AP009048
PIR B25024
RefSeq NP_417863.1
YP_492028.1
PDB 1BXD
1JOY
1NJV
3ZCC
3ZRV
3ZRW
3ZRX
4CTI
4KP4
PDBsum 1BXD
1JOY
1NJV
3ZCC
3ZRV
3ZRW
3ZRX
4CTI
4KP4
ProteinModelPortal P0AEJ4
SMR P0AEJ4
DIP DIP-48357N
IntAct P0AEJ4
MINT MINT-8398485
STRING 511145.b3404
EnsemblBacteria AAC76429
BAE77887
GeneID 12932272
947272
KEGG ecj:Y75_p3772
eco:b3404
PATRIC 32122244
EchoBASE EB0265
EcoGene EG10269
eggNOG COG0642
HOGENOM HOG000218774
InParanoid P0AEJ4
KO K07638
OMA WIRPPQA
OrthoDB EOG6G4VQG
PhylomeDB P0AEJ4
BioCyc EcoCyc:ENVZ-MONOMER
ECOL316407:JW3367-MONOMER
EvolutionaryTrace P0AEJ4
PRO PR:P0AEJ4
Proteomes UP000000318
UP000000625
Genevestigator P0AEJ4
GO GO:0009898
GO:0005887
GO:0005524
GO:0004721
GO:0000155
GO:0016048
GO:0000160
GO:0016310
GO:0046777
GO:0006470
GO:0047484
GO:0023014
Gene3D 1.10.287.130
3.30.565.10
InterPro IPR003661
IPR003660
IPR003594
IPR004358
IPR005467
IPR009082
Pfam PF00672
PF02518
PF00512
PRINTS PR00344
SMART SM00304
SM00387
SM00388
SUPFAM SSF47384
SSF55874
PROSITE PS50885
PS50109

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0046777

protein autophosphorylation

PMID:10973966[1]

ECO:0000315

P

EnvZ mutants cannot properly autophosphorylate in Fig 3.

complete
CACAO 4641

GO:0016301

kinase activity

PMID:10973966[1]

ECO:0000314

F

Figure 4 and Figure 5. Phosphotransfer from phosphorylated EnvZc and EnvZc(T247X) mutant proteins to OmpR.A. EnvZ-P, phosphorylated EnvZ.


complete
CACAO 4647

GO:0006470

protein dephosphorylation

PMID:2656684[2]

ECO:0000314

P

FIG. 7. Autoradiograms showing the time course of dephosphorylation of EnvZ* mediated by a substoichiometric amount of OmpR.

complete
CACAO 4660

GO:0071229

cellular response to acid

PMID:20380141[3]

ECO:0000315

P

Figures 1-5 shows growth rates,and correlation, as the PH increased, survival times for wild type decreased. ensZ mutants survived better than other mutants.

complete
CACAO 4672

GO:0004721

phosphoprotein phosphatase activity

PMID:10973966[1]

ECO:0000315

F

figure 7 shows phosphatase activity of mutants relative to wild type

complete
CACAO 4686

involved_in

GO:0046777

protein autophosphorylation

PMID:10973966[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0047484

regulation of response to osmotic stress

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10269
PANTHER:PTN001293174

P

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10269
PANTHER:PTN001293174

C

Seeded From UniProt

complete

enables

GO:0000155

phosphorelay sensor kinase activity

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10269
EcoGene:EG10730
PANTHER:PTN001293174

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19432797[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AEJ4

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:10426948[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AEJ4

F

Seeded From UniProt

complete

involved_in

GO:0046777

protein autophosphorylation

PMID:2558046[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

PMID:2558046[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006470

protein dephosphorylation

PMID:2558046[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000160

phosphorelay signal transduction system

PMID:2558046[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0047484

regulation of response to osmotic stress

PMID:3536870[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0023014

signal transduction by protein phosphorylation

PMID:2558046[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009898

cytoplasmic side of plasma membrane

PMID:2824492[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:2824492[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004721

phosphoprotein phosphatase activity

PMID:2558046[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000155

phosphorelay sensor kinase activity

PMID:2668953[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0018106

peptidyl-histidine phosphorylation

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004673

P

Seeded From UniProt

complete

enables

GO:0000155

phosphorelay sensor kinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003661
InterPro:IPR036097

F

Seeded From UniProt

complete

involved_in

GO:0007165

signal transduction

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003660
InterPro:IPR003661
InterPro:IPR036097

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003660

C

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004358

P

Seeded From UniProt

complete

enables

GO:0016772

transferase activity, transferring phosphorus-containing groups

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004358

F

Seeded From UniProt

complete

enables

GO:0004673

protein histidine kinase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.13.3

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0997
UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

involved_in

GO:0000160

phosphorelay signal transduction system

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0902

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Dutta, R et al. (2000) The critical role of the conserved Thr247 residue in the functioning of the osmosensor EnvZ, a histidine Kinase/Phosphatase, in Escherichia coli. J. Biol. Chem. 275 38645-53 PubMed GONUTS page
  2. Aiba, H et al. (1989) Transfer of phosphoryl group between two regulatory proteins involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli. J. Biol. Chem. 264 8563-7 PubMed GONUTS page
  3. Darcan, C et al. (2009) Viable but non-culturable state (VBNC) of Escherichia coli related to EnvZ under the effect of pH, starvation and osmotic stress in sea water. Pol. J. Microbiol. 58 307-17 PubMed GONUTS page
  4. 4.0 4.1 4.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  5. Gerken, H et al. (2009) MzrA: a novel modulator of the EnvZ/OmpR two-component regulon. Mol. Microbiol. 72 1408-22 PubMed GONUTS page
  6. Tomomori, C et al. (1999) Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ. Nat. Struct. Biol. 6 729-34 PubMed GONUTS page
  7. 7.0 7.1 7.2 7.3 7.4 7.5 Igo, MM et al. (1989) Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor. Genes Dev. 3 1725-34 PubMed GONUTS page
  8. Matsuyama, S et al. (1986) Interaction between two regulatory proteins in osmoregulatory expression of ompF and ompC genes in Escherichia coli: a novel ompR mutation suppresses pleiotropic defects caused by an envZ mutation. J. Bacteriol. 168 1309-14 PubMed GONUTS page
  9. 9.0 9.1 Forst, S et al. (1987) Localization and membrane topology of EnvZ, a protein involved in osmoregulation of OmpF and OmpC in Escherichia coli. J. Biol. Chem. 262 16433-8 PubMed GONUTS page
  10. Forst, S et al. (1989) Phosphorylation of OmpR by the osmosensor EnvZ modulates expression of the ompF and ompC genes in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 86 6052-6 PubMed GONUTS page