Difference between revisions of "GlnA"
(→Biological materials) |
|||
Line 18: | Line 18: | ||
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1332 bp, 444 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1332 bp, 444 aa | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[glnR]]'', ''[[ynxB]]'' |
|- | |- | ||
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/glnA_nucleotide.txt Gene sequence (+200bp) ]''' | |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/glnA_nucleotide.txt Gene sequence (+200bp) ]''' |
Revision as of 15:32, 20 February 2009
- Description: glutamine synthetase
Gene name | glnA |
Synonyms | |
Essential | no |
Product | glutamine synthetase (EC 6.3.1.2) |
Function | |
MW, pI | 50 kDa, 4.874 |
Gene length, protein length | 1332 bp, 444 aa |
Immediate neighbours | glnR, ynxB |
Gene sequence (+200bp) | Protein sequence |
Genetic context |
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
auxotrophic for glutamine
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:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry:
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation: expressed in the absence of glutamine PubMed
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody: available in Karl Forchhammer lab
Labs working on this gene/protein
Susan Fisher, Boston, USA homepage
Your additional remarks
References
- Brown, S. W., and A. L. Sonenshein. 1996. Autogenous regulation of the Bacillus subtilis glnRA operon. J. Bacteriol. 178: 2450-2454. PubMed
- Wray LV Jr, Zalieckas JM, Fisher SH. (2001) Bacillus subtilis glutamine synthetase controls gene expression through protein-protein interaction with transcription factor TnrA. Cell 107:427-435. PubMed
- Fisher, S. H., and Wray, L. V., Jr. (2006) Feedback-resistant mutations in Bacillus subtilis glutamine synthetase are clustered in the active site. J Bacteriol 188: 5966-5974. PubMed
- Fisher SH, Sonenshein AL (1984) Bacillus subtilis glutamine synthetase mutants pleiotropically altered in catabolite repression. J Bacteriol 157:612-621. PubMed
- Fisher, S. H., Brandenburg, J. L. & Wray, L. V. (2002). Mutations in Bacillus subtilis glutamine synthetase that block its interaction with transcription factor TnrA. Mol Microbiol 45, 627-635. PubMed
- Schreier, H. J., Brown, S. W., Hirschi, K. D., Nomellini, J. F. & Sonenshein, A. L. (1989). Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene. J Mol Biol 210, 51-63. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed