Difference between revisions of "TnrA"

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|style="background:#ABCDEF;" align="center"|'''Function''' ||regulation of nitrogen assimilation <br/>(positive regulation of nrgAB, nasBCDEF, gabP,<br/> ureABC, guaD; negative regulation of glnRA, gltAB)
 
|style="background:#ABCDEF;" align="center"|'''Function''' ||regulation of nitrogen assimilation <br/>(positive regulation of nrgAB, nasBCDEF, gabP,<br/> ureABC, guaD; negative regulation of glnRA, gltAB)
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/gene_regulation_nucleotides.html Nucleotides (regulation)], [http://subtiwiki.uni-goettingen.de/pathways/ile_val_leu.html Ile, Leu, Val], [http://subtiwiki.uni-goettingen.de/pathways/glutamate.html Ammonium/ glutamate],<br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism], [http://subtiwiki.uni-goettingen.de/pathways/cellwall.html Cell wall], [http://subtiwiki.uni-goettingen.de/pathways/CoA_synthesis.html Coenzyme A]'''
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_syn.html Lipid synthesis], [http://subtiwiki.uni-goettingen.de/pathways/gene_regulation_nucleotides.html Nucleotides (regulation)], [http://subtiwiki.uni-goettingen.de/pathways/ile_val_leu.html Ile, Leu, Val], [http://subtiwiki.uni-goettingen.de/pathways/glutamate.html Ammonium/ glutamate],<br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism], [http://subtiwiki.uni-goettingen.de/pathways/cellwall.html Cell wall], [http://subtiwiki.uni-goettingen.de/pathways/CoA_synthesis.html Coenzyme A]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 12 kDa, 10.235   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 12 kDa, 10.235   

Revision as of 13:43, 16 February 2010

  • 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:
Lipid synthesis, 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
TnrA context.gif
This image was kindly provided by SubtiList








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
  • Localization:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon: tnrA (according to DBTBS)
  • Regulation:
    • expression is autocativated (TnrA) and repressed by GlnR PubMed
    • expressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP252 (in frame deletion), available in the Stülke lab
  • Expression vector:
    • for expression, purification in E. coli with N-terminal His-tag, in pWH844: pGP171 available in Stülke lab
    • pGP229 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:

Labs working on this gene/protein

Susan Fisher, Boston, USA homepage

Your additional remarks

References

Reviews

Fabian M Commichau, Jörg Stülke
Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression.
Mol Microbiol: 2008, 67(4);692-702
[PubMed:18086213] [WorldCat.org] [DOI] (P p)

S H Fisher
Regulation of nitrogen metabolism in Bacillus subtilis: vive la différence!
Mol Microbiol: 1999, 32(2);223-32
[PubMed:10231480] [WorldCat.org] [DOI] (P p)

Original publications