Difference between revisions of "TnrA"
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− | 2573733, 8636055, 19233925, 16493705, 16885465, 6141156</pubmed> | + | 2573733, 8636055, 19233925, 16493705, 16885465, 6141156 18667567 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 08:35, 22 September 2009
- Description: transcriptional pleiotropic regulator invoved in global nitrogen regulation
Gene name | tnrA |
Synonyms | scgR |
Essential | no |
Product | transcription activator/ repressor |
Function | regulation of nitrogen assimilation (positive regulation of nrgAB, nasBCDEF, gabP, ureABC, guaD; negative regulation of glnRA, gltAB) |
Metabolic function and regulation of this protein in SubtiPathways: Nucleotides (regulation), Ile, Leu, Val, Ammonium/ glutamate, Central C-metabolism, Cell wall, Coenzyme A | |
MW, pI | 12 kDa, 10.235 |
Gene length, protein length | 330 bp, 110 aa |
Immediate neighbours | mgtE, ykzB |
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: BSU13310
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):
Genes/ operons controlled by TnrA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: feedback-inhibited GlnA prevents TnrA from DNA binding
- Interactions: TnrA-GlnA, TnrA-NrgB PubMed, TnrA-GlnA, this interaction results in loss of TnrA DNA-binding activity
- Localization:
Database entries
- Structure:
- UniProt: Q45666
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Additional information:
Biological materials
- Mutant: GP243 (cat), GP252 (in frame deletion), available in the Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody: available in the Karl Forchhammer lab
Labs working on this gene/protein
Susan Fisher, Boston, USA homepage
Your additional remarks
References