Difference between revisions of "PhoR"
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' autophosphorylation, phosphorylation of [[PhoP]] |
* '''Protein family:''' | * '''Protein family:''' | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
− | * '''Domains:''' | + | * '''Domains:''' two transmembrane segments, C-terminal histidine phosphotransferase domain |
− | * '''Modification:''' | + | * '''Modification:''' autophosphorylation on a His residue |
* '''Cofactor(s):''' | * '''Cofactor(s):''' |
Revision as of 19:38, 30 November 2009
- Description: two-component sensor kinase, regulation of phosphate metabolism
Gene name | phoR |
Synonyms | |
Essential | no |
Product | two-component sensor kinase |
Function | regulation of phosphate metabolism |
MW, pI | 64 kDa, 5.957 |
Gene length, protein length | 1737 bp, 579 aa |
Immediate neighbours | polA, phoP |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU29100
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: autophosphorylation, phosphorylation of PhoP
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains: two transmembrane segments, C-terminal histidine phosphotransferase domain
- Modification: autophosphorylation on a His residue
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure: 3CWF
- UniProt: P23545
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Marion Hulett, University of Illinois at Chicago, USA Homepage
Your additional remarks
References