Difference between revisions of "AhrC"
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= |
Revision as of 12:25, 26 January 2012
- Description: AhrC represses the genes for arginine biosynthesis and activates the genes for arginine catabolism.
Gene name | ahrC |
Synonyms | argR |
Essential | no |
Product | transcriptional regulator |
Function | transcriptional regulator of arginine metabolic genes |
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate | |
MW, pI | 16,7 kDa, 5.52 |
Gene length, protein length | 447 bp, 149 amino acids |
Immediate neighbours | recN, yqxC |
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, utilization of amino acids, transcription factors and their control
This gene is a member of the following regulons
The AhrC regulon
The gene
Basic information
- Locus tag: BSU24250
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: transcriptional activator/ repressor of genes involved in arginine metabolism
- Protein family: argR family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s): L-arginine is the co-factor required for transcription repression/ activation
- Effectors of protein activity:
- Localization: Cytoplasm
Database entries
- Structure: 2P5M (C-Terminus), 2P5K (complex with an 18bp DNA operator), 2P5L (N-terminus), 1F9N, NCBI PubMed,N-Terminus NCBI, C-Terminus NCBI, complex with an 18bp DNA operator NCBI
- UniProt: P17893
- KEGG entry: [3]
Additional information
Expression and regulation
- Sigma factor:
- Additional information:
Biological materials
- Mutant: GP729 (aphA3), available in Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- Antibody:
Labs working on this gene/protein
Simon Phillips, Leeds University, UK Homepage
Michel Debarbouille, Pasteur Institute, Paris, France Homepage
Your additional remarks
References
James A Garnett, Ferenc Marincs, Simon Baumberg, Peter G Stockley, Simon E V Phillips
Structure and function of the arginine repressor-operator complex from Bacillus subtilis.
J Mol Biol: 2008, 379(2);284-98
[PubMed:18455186]
[WorldCat.org]
[DOI]
(I p)
James A Garnett, Simon Baumberg, Peter G Stockley, Simon E V Phillips
Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2007, 63(Pt 11);918-21
[PubMed:18007040]
[WorldCat.org]
[DOI]
(I p)
James A Garnett, Simon Baumberg, Peter G Stockley, Simon E V Phillips
A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2007, 63(Pt 11);914-7
[PubMed:18007039]
[WorldCat.org]
[DOI]
(I p)
Nadja Heidrich, Isabella Moll, Sabine Brantl
In vitro analysis of the interaction between the small RNA SR1 and its primary target ahrC mRNA.
Nucleic Acids Res: 2007, 35(13);4331-46
[PubMed:17576690]
[WorldCat.org]
[DOI]
(I p)
Nadja Heidrich, Alberto Chinali, Ulf Gerth, Sabine Brantl
The small untranslated RNA SR1 from the Bacillus subtilis genome is involved in the regulation of arginine catabolism.
Mol Microbiol: 2006, 62(2);520-36
[PubMed:17020585]
[WorldCat.org]
[DOI]
(P p)
Caitríona A Dennis C, Nicholas M Glykos, Mark R Parsons, Simon E V Phillips
The structure of AhrC, the arginine repressor/activator protein from Bacillus subtilis.
Acta Crystallogr D Biol Crystallogr: 2002, 58(Pt 3);421-30
[PubMed:11856827]
[WorldCat.org]
[DOI]
(P p)
K S Makarova, A A Mironov, M S Gelfand
Conservation of the binding site for the arginine repressor in all bacterial lineages.
Genome Biol: 2001, 2(4);RESEARCH0013
[PubMed:11305941]
[WorldCat.org]
[DOI]
(I p)
C M Miller, S Baumberg, P G Stockley
Operator interactions by the Bacillus subtilis arginine repressor/activator, AhrC: novel positioning and DNA-mediated assembly of a transcriptional activator at catabolic sites.
Mol Microbiol: 1997, 26(1);37-48
[PubMed:9383188]
[WorldCat.org]
[DOI]
(P p)
U Klingel, C M Miller, A K North, P G Stockley, S Baumberg
A binding site for activation by the Bacillus subtilis AhrC protein, a repressor/activator of arginine metabolism.
Mol Gen Genet: 1995, 248(3);329-40
[PubMed:7565595]
[WorldCat.org]
[DOI]
(P p)
L G Czaplewski, A K North, M C Smith, S Baumberg, P G Stockley
Purification and initial characterization of AhrC: the regulator of arginine metabolism genes in Bacillus subtilis.
Mol Microbiol: 1992, 6(2);267-75
[PubMed:1312212]
[WorldCat.org]
[DOI]
(P p)
B E Van Hoy, J A Hoch
Characterization of the spoIVB and recN loci of Bacillus subtilis.
J Bacteriol: 1990, 172(3);1306-11
[PubMed:2106508]
[WorldCat.org]
[DOI]
(P p)