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ECOBW:C4ZUQ9
Contents
| Species (Taxon ID) | Escherichia coli (strain K12 / MC4100 / BW2952). (595496) | |
| Gene Name(s) | envZ (ECO:0000313 with EMBL:ACR65530.1) | |
| Protein Name(s) | Sensory histidine kinase in two-component regulatory system with OmpR (ECO:0000313 with EMBL:ACR65530.1) | |
| External Links | ||
| UniProt | C4ZUQ9 | |
| EMBL | CP001396 | |
| RefSeq | YP_002928291.1 | |
| ProteinModelPortal | C4ZUQ9 | |
| SMR | C4ZUQ9 | |
| STRING | 595496.BWG_3095 | |
| EnsemblBacteria | ACR65530 | |
| GeneID | 7954528 | |
| KEGG | ebw:BWG_3095 | |
| PATRIC | 18275778 | |
| eggNOG | COG0642 | |
| HOGENOM | HOG000218774 | |
| KO | K07638 | |
| OMA | WIRPPQA | |
| OrthoDB | EOG6G4VQG | |
| BioCyc | ECOL595496:GI18-3219-MONOMER | |
| Proteomes | UP000001478 | |
| GO | GO:0016021 GO:0005524 GO:0000155 | |
| 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 | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
Contributes to |
GO:0000155 |
two-component sensor activity |
IDA: Inferred from Direct Assay |
F |
Figure 6: Shows that competition exists between Fl-OmpR and OmpR-P for binding to EnvZc. |
complete | ||
|
Contributes to |
GO:0000155 |
two-component sensor activity |
IMP: Inferred from Mutant Phenotype |
F |
Figure 6: Shows that competition exists between Fl-OmpR and OmpR-P for binding to EnvZc. |
complete | ||
|
Contributes to |
GO:0000155 |
two-component sensor activity |
IMP: Inferred from Mutant Phenotype |
F |
Figure 6: Shows that competition exists between Fl-OmpR and OmpR-P for binding to EnvZc. |
complete | ||
| GO:0000155 |
phosphorelay sensor kinase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
complete | |||
|
Contributes to |
GO:0000155 |
PMID:PMID:12453215[1] |
IMP: Inferred from Mutant Phenotype |
Figure 6: Shows that competition exists between Fl-OmpR and OmpR-P for binding to EnvZc. |
complete | |||
| GO:0000160 |
phosphorelay signal transduction system |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
complete | |||
| GO:0000166 |
nucleotide binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
complete | |||
|
Contributes to |
GO:0016310 |
phosphorylation |
PMID:PMC2853374 |
IDA: Inferred from Direct Assay |
P |
Figure 2: At low osmolality, the level of intracellular OmpR~P is low either because the kinase activity of EnvZ is low, or because EnvZ phosphatase activity is high. At high osmolality OmpR~P levels increase either because of an increase in the EnvZ kinase activity or a decrease in EnvZ phosphatase activity. |
complete | |
| GO:0004871 |
signal transducer activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
complete | |||
|
Contributes to |
GO:0016310 |
phosphorylation |
PMID:PMC2853374 |
IMP: Inferred from Mutant Phenotype |
P |
Figure 2: At low osmolality, the level of intracellular OmpR~P is low either because the kinase activity of EnvZ is low, or because EnvZ phosphatase activity is high. At high osmolality OmpR~P levels increase either because of an increase in the EnvZ kinase activity or a decrease in EnvZ phosphatase activity. |
complete | |
| GO:0005524 |
ATP binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
complete | |||
|
Contributes to |
GO:0016310 |
phosphorylation |
IDA: Inferred from Direct Assay |
P |
Figure 2: At low osmolality, the level of intracellular OmpR~P is low either because the kinase activity of EnvZ is low, or because EnvZ phosphatase activity is high. At high osmolality OmpR~P levels increase either because of an increase in the EnvZ kinase activity or a decrease in EnvZ phosphatase activity. |
complete | ||
| GO:0005524 |
ATP binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
complete | |||
| GO:0007165 |
signal transduction |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
complete | |||
|
Contributes to |
GO:0016310 |
phosphorylation |
IDA: Inferred from Direct Assay |
P |
Figure 2: At low osmolality, the level of intracellular OmpR~P is low either because the kinase activity of EnvZ is low, or because EnvZ phosphatase activity is high. At high osmolality OmpR~P levels increase either because of an increase in the EnvZ kinase activity or a decrease in EnvZ phosphatase activity. |
complete | ||
|
Contributes to |
GO:0005524 |
ATP binding |
IDA: Inferred from Direct Assay |
F |
Figure 5: ATPase assay measured OmpR-stimulated ATPase activity represent the sum of the phosphorylation/phosphotransfer reactions. |
complete | ||
| GO:0016020 |
membrane |
IEA: Inferred from Electronic Annotation |
C |
Seeded From UniProt |
complete | |||
|
Contributes to |
GO:0005524 |
ATP binding |
IMP: Inferred from Mutant Phenotype |
F |
Figure 5: ATPase assay measured OmpR-stimulated ATPase activity represent the sum of the phosphorylation/phosphotransfer reactions. |
complete | ||
| GO:0016020 |
membrane |
IEA: Inferred from Electronic Annotation |
C |
Seeded From UniProt |
complete | |||
|
Contributes to |
GO:0016020 |
membrane |
IDA: Inferred from Direct Assay |
C |
Figure 3: Shows the mapping of the membrane-binding surface of NRne in E. coli. Data suggests the existence of a positively charged surface that mediates interaction of NRne with the inner membrane. |
complete | ||
| GO:0016021 |
integral component of membrane |
IEA: Inferred from Electronic Annotation |
C |
Seeded From UniProt |
complete | |||
|
Contributes to |
GO:0016020 |
IMP: Inferred from Mutant Phenotype |
Figure 3: Shows the mapping of the membrane-binding surface of NRne in E. coli. Data suggests the existence of a positively charged surface that mediates interaction of NRne with the inner membrane. |
complete | ||||
| GO:0016021 |
integral component of membrane |
IEA: Inferred from Electronic Annotation |
C |
Seeded From UniProt |
complete | |||
| GO:0016301 |
kinase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
complete | |||
| GO:0016310 |
phosphorylation |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
complete | |||
| GO:0016310 |
phosphorylation |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
complete | |||
| GO:0016740 |
transferase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
complete | |||
| GO:0016772 |
transferase activity, transferring phosphorus-containing groups |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
complete | |||
| GO:0023014 |
signal transduction by protein phosphorylation |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 Yoshida, T et al. (2002) Interaction of EnvZ, a sensory histidine kinase, with phosphorylated OmpR, the cognate response regulator. Mol. Microbiol. 46 1283-94 PubMed GONUTS page
- ↑ Michela, WA (1976) Cost of labor. Hospitals 50 46 PubMed GONUTS page
- ↑ Watson, PJ & Leitner, C (1988) Patterns of increased and decreased ingestive behavior after injections of lithium chloride and 2-deoxy-D-glucose. Physiol. Behav. 43 697-704 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 Kenney, LJ (2010) How important is the phosphatase activity of sensor kinases? Curr. Opin. Microbiol. 13 168-76 PubMed GONUTS page
- ↑ 5.0 5.1 Murashko, ON et al. (2012) Membrane binding of Escherichia coli RNase E catalytic domain stabilizes protein structure and increases RNA substrate affinity. Proc. Natl. Acad. Sci. U.S.A. 109 7019-24 PubMed GONUTS page
