Difference between revisions of "TnrA"
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|style="background:#ABCDEF;" align="center"| '''Product''' || transcription activator/ repressor | |style="background:#ABCDEF;" align="center"| '''Product''' || transcription activator/ repressor | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' ||regulation of nitrogen assimilation | + | |style="background:#ABCDEF;" align="center"|'''Function''' ||regulation of nitrogen assimilation |
|- | |- | ||
|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_synthesis.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], <br/>[http://subtiwiki.uni-goettingen.de/pathways/glutamate.html Ammonium/ glutamate], [http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism], [http://subtiwiki.uni-goettingen.de/pathways/cellwall.html Cell wall], <br/>[http://subtiwiki.uni-goettingen.de/pathways/CoA_synthesis.html Coenzyme A], [http://subtiwiki.uni-goettingen.de/pathways/phosphorelay.html Phosphorelay], [http://subtiwiki.uni-goettingen.de/pathways/other_nitrogen_sources/index.html Alternative nitrogen sources]''' | |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_synthesis.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], <br/>[http://subtiwiki.uni-goettingen.de/pathways/glutamate.html Ammonium/ glutamate], [http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism], [http://subtiwiki.uni-goettingen.de/pathways/cellwall.html Cell wall], <br/>[http://subtiwiki.uni-goettingen.de/pathways/CoA_synthesis.html Coenzyme A], [http://subtiwiki.uni-goettingen.de/pathways/phosphorelay.html Phosphorelay], [http://subtiwiki.uni-goettingen.de/pathways/other_nitrogen_sources/index.html Alternative nitrogen sources]''' | ||
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{{SubtiWiki regulon|[[GlnR regulon]]}}, | {{SubtiWiki regulon|[[GlnR regulon]]}}, | ||
{{SubtiWiki regulon|[[TnrA regulon]]}} | {{SubtiWiki regulon|[[TnrA regulon]]}} | ||
− | + | =The [[TnrA regulon]]= | |
=The gene= | =The gene= | ||
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=== Additional information=== | === Additional information=== | ||
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− | |||
− | |||
=The protein= | =The protein= | ||
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* '''Paralogous protein(s):''' | * '''Paralogous protein(s):''' | ||
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=== Extended information on the protein === | === Extended information on the protein === | ||
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==Reviews== | ==Reviews== | ||
<pubmed> 10231480 18086213 </pubmed> | <pubmed> 10231480 18086213 </pubmed> | ||
− | == | + | ==The [[TnrA regulon]]== |
− | <pubmed>12374841,15547269,9287005 | + | <pubmed>12823818,</pubmed> |
− | 2573733, 8636055 | + | ==Control of TnrA activity by the [[trigger enzymes|trigger enzyme]] [[GlnA]]== |
+ | <pubmed>11719184, 12139611, 17085574 19233925, 16885465, </pubmed> | ||
+ | ==Other original publications== | ||
+ | <pubmed>12374841,15547269,9287005, 12950915,10671441,16547045,16547045 ,8799114, 15150225, 11029411,17001076,15547269, 2573733, 8636055, 16493705, 6141156 18667567 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 20:13, 4 January 2011
- 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 |
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, Phosphorelay, Alternative nitrogen sources | |
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
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, regulators of core metabolism
This gene is a member of the following regulons
The TnrA regulon
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):
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-NrgB PubMed, TnrA-GlnA, this interaction results in loss of TnrA DNA-binding activity PubMed
- Localization:
Database entries
- Structure:
- UniProt: Q45666
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: tnrA (according to DBTBS)
- Regulation:
- Additional information:
Biological materials
- Mutant: 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
Reviews
The TnrA regulon
Control of TnrA activity by the trigger enzyme GlnA
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
Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein.
J Bacteriol: 2007, 189(1);20-7
[PubMed:17085574]
[WorldCat.org]
[DOI]
(P p)
Susan H Fisher, Lewis V Wray
Feedback-resistant mutations in Bacillus subtilis glutamine synthetase are clustered in the active site.
J Bacteriol: 2006, 188(16);5966-74
[PubMed:16885465]
[WorldCat.org]
[DOI]
(P p)
Susan H Fisher, Jaclyn L Brandenburg, Lewis V Wray
Mutations in Bacillus subtilis glutamine synthetase that block its interaction with transcription factor TnrA.
Mol Microbiol: 2002, 45(3);627-35
[PubMed:12139611]
[WorldCat.org]
[DOI]
(P p)
L V Wray, J M Zalieckas, S H Fisher
Bacillus subtilis glutamine synthetase controls gene expression through a protein-protein interaction with transcription factor TnrA.
Cell: 2001, 107(4);427-35
[PubMed:11719184]
[WorldCat.org]
[DOI]
(P p)
Other original publications