Difference between revisions of "GlnR"
(→Biological materials) |
|||
Line 68: | Line 68: | ||
* '''Modification:''' | * '''Modification:''' | ||
− | * '''Cofactor(s):''' feedback-inhibited [[GlnA]] | + | * '''Cofactor(s):''' feedback-inhibited [[GlnA]] {{PubMed|18195355}} |
− | * '''Effectors of protein activity:''' | + | * '''Effectors of protein activity:''' activity is enhanced upon interaction of the C-terminal domain with [[GlnA]] {{PubMed|18195355}} |
− | * '''Interactions:''' [[GlnR]]-[[GlnA]], with feedback-inhibited [[GlnA]], this results in DNA binding | + | * '''Interactions:''' [[GlnR]]-[[GlnA]], with feedback-inhibited [[GlnA]], this results in DNA binding {{PubMed|18195355}} |
* '''Localization:''' | * '''Localization:''' |
Revision as of 18:57, 31 July 2010
Gene name | glnR |
Synonyms | |
Essential | no |
Product | transcription repressor |
Function | regulation of glutamine synthesis |
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate, Cell wall | |
MW, pI | 15 kDa, 9.731 |
Gene length, protein length | 405 bp, 135 aa |
Immediate neighbours | ynbB, glnA |
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: BSU17450
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Effectors of protein activity: activity is enhanced upon interaction of the C-terminal domain with GlnA PubMed
- Localization:
Database entries
- Structure:
- UniProt: P37582
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Susan Fisher, Boston, USA homepage
Your additional remarks
References