Difference between revisions of "GlnR"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=glnR_1877959_1878366_1 glnR] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=glnR_1877959_1878366_1 glnR] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' [[SigA]] {{PubMed|2906311}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|2906311}} |
* '''Regulation:''' | * '''Regulation:''' | ||
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=References= | =References= | ||
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==Original publications== | ==Original publications== | ||
<pubmed>12374841,9287005,8799114, 18195355, 2573733, 8636055, 19233925 2906311 18331450 16547045 </pubmed> | <pubmed>12374841,9287005,8799114, 18195355, 2573733, 8636055, 19233925 2906311 18331450 16547045 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 14:10, 28 March 2013
Gene name | glnR |
Synonyms | |
Essential | no |
Product | transcription repressor |
Function | regulation of glutamine synthesis |
Gene expression levels in SubtiExpress: glnR | |
Interactions involving this protein in SubtInteract: GlnR | |
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate, Cell wall, Alternative nitrogen sources | |
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
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, glutamate metabolism, transcription factors and their control
This gene is a member of the following regulons
The GlnR regulon:
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
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
Reviews
Katrin Gunka, Fabian M Commichau
Control of glutamate homeostasis in Bacillus subtilis: a complex interplay between ammonium assimilation, glutamate biosynthesis and degradation.
Mol Microbiol: 2012, 85(2);213-24
[PubMed:22625175]
[WorldCat.org]
[DOI]
(I p)
Original publications
Susan H Fisher, Lewis V Wray
Novel trans-Acting Bacillus subtilis glnA mutations that derepress glnRA expression.
J Bacteriol: 2009, 191(8);2485-92
[PubMed:19233925]
[WorldCat.org]
[DOI]
(I p)
Lewis V Wray, Susan H Fisher
Bacillus subtilis GlnR contains an autoinhibitory C-terminal domain required for the interaction with glutamine synthetase.
Mol Microbiol: 2008, 68(2);277-85
[PubMed:18331450]
[WorldCat.org]
[DOI]
(I p)
Susan H Fisher, Lewis V Wray
Bacillus subtilis glutamine synthetase regulates its own synthesis by acting as a chaperone to stabilize GlnR-DNA complexes.
Proc Natl Acad Sci U S A: 2008, 105(3);1014-9
[PubMed:18195355]
[WorldCat.org]
[DOI]
(I p)
Jill M Zalieckas, Lewis V Wray, Susan H Fisher
Cross-regulation of the Bacillus subtilis glnRA and tnrA genes provides evidence for DNA binding site discrimination by GlnR and TnrA.
J Bacteriol: 2006, 188(7);2578-85
[PubMed:16547045]
[WorldCat.org]
[DOI]
(P p)
Jaclyn L Brandenburg, Lewis V Wray, Lars Beier, Hanne Jarmer, Hans H Saxild, Susan H Fisher
Roles of PucR, GlnR, and TnrA in regulating expression of the Bacillus subtilis ure P3 promoter.
J Bacteriol: 2002, 184(21);6060-4
[PubMed:12374841]
[WorldCat.org]
[DOI]
(P p)
L V Wray, A E Ferson, S H Fisher
Expression of the Bacillus subtilis ureABC operon is controlled by multiple regulatory factors including CodY, GlnR, TnrA, and Spo0H.
J Bacteriol: 1997, 179(17);5494-501
[PubMed:9287005]
[WorldCat.org]
[DOI]
(P p)
L V Wray, A E Ferson, K Rohrer, S H Fisher
TnrA, a transcription factor required for global nitrogen regulation in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1996, 93(17);8841-5
[PubMed:8799114]
[WorldCat.org]
[DOI]
(P p)
S W Brown, A L Sonenshein
Autogenous regulation of the Bacillus subtilis glnRA operon.
J Bacteriol: 1996, 178(8);2450-4
[PubMed:8636055]
[WorldCat.org]
[DOI]
(P p)
H J Schreier, S W Brown, K D Hirschi, J F Nomellini, A L Sonenshein
Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene.
J Mol Biol: 1989, 210(1);51-63
[PubMed:2573733]
[WorldCat.org]
[DOI]
(P p)
M A Strauch, A I Aronson, S W Brown, H J Schreier, A L Sonenhein
Sequence of the Bacillus subtilis glutamine synthetase gene region.
Gene: 1988, 71(2);257-65
[PubMed:2906311]
[WorldCat.org]
[DOI]
(P p)