GlnA

• Description: glutamine synthetase
  
  

Gene name	glnA
Synonyms
Essential	no
Product	trigger enzyme: glutamine synthetase
Function	glutamine biosynthesis, control of TnrA and GlnR activity
MW, pI	50 kDa, 4.874
Gene length, protein length	1332 bp, 444 aa
Immediate neighbours	glnR, ynxB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates:

Phenotypes of a mutant

auxotrophic for glutamine

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information: K(M) for: Glu: 27 mM, ATP: 2.4 mM, ammonium: 0.18 mM; v(max): 3.7 µmol/min/mg

• Domains: glutamate binding flap (aa 300 ... 306: protects unstable intermediates from abberant hydrolysis)

• Modification: phosphorylated on ser/ thr/ tyr PubMed

• Cofactor(s): Mg(2+)

• Effectors of protein activity: feedback inhibition by glutamine, glutamine binds thhe entrance site for glutamate

• Interactions: GlnR-GlnA, GlnR-GlnA, GlnA-TnrA (only the feedback-inhibited enzyme interacts with TnrA and GlnR)

• Localization:

Database entries

• Structure:

• Swiss prot entry:

• KEGG entry: [3]

• E.C. number: 6.3.1.2

Additional information

GlnA is a homooligomer of 12 subunits

Expression and regulation

• Operon: glnR-glnA PubMed

• Sigma factor: SigA

• Regulation: expressed in the absence of glutamine PubMed

• Regulatory mechanism: repressed by GlnR-GlnA complex 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

References

1. Lévine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6: 2157-2173 PubMed
2. Brown, S. W., and A. L. Sonenshein. 1996. Autogenous regulation of the Bacillus subtilis glnRA operon. J. Bacteriol. 178: 2450-2454. PubMed
3. 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
4. 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
5. Fisher SH, Sonenshein AL (1984) Bacillus subtilis glutamine synthetase mutants pleiotropically altered in catabolite repression. J Bacteriol 157:612-621. PubMed
6. 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
7. 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
8. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed