Difference between revisions of "MurAA"
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=== Additional information=== | === Additional information=== | ||
| + | :* subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | ||
MurAA is subject to [[ClpC]]-[[ClpP]]-dependent degradation [http://www.ncbi.nlm.nih.gov/sites/entrez/14763982 PubMed] | MurAA is subject to [[ClpC]]-[[ClpP]]-dependent degradation [http://www.ncbi.nlm.nih.gov/sites/entrez/14763982 PubMed] | ||
| Line 101: | Line 102: | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| − | * '''Additional information:''' | + | * '''Additional information:''' subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] |
=Biological materials = | =Biological materials = | ||
| Line 123: | Line 124: | ||
=References= | =References= | ||
| + | # Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | ||
# Kock H, Gerth U, Hecker M. (2004) MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis. Mol Microbiol, 51:1087-1102. [http://www.ncbi.nlm.nih.gov/sites/entrez/14763982 PubMed] | # Kock H, Gerth U, Hecker M. (2004) MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis. Mol Microbiol, 51:1087-1102. [http://www.ncbi.nlm.nih.gov/sites/entrez/14763982 PubMed] | ||
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | ||
Revision as of 11:53, 27 March 2009
- Description: UDP-N-acetylglucosamine 1-carboxyvinyltransferase
| Gene name | murAA |
| Synonyms | murA |
| Essential | yes PubMed |
| Product | UDP-N-acetylglucosamine 1-carboxyvinyltransferase |
| Function | peptidoglycan precursor biosynthesis |
| MW, pI | 46 kDa, 5.45 |
| Gene length, protein length | 1308 bp, 436 aa |
| Immediate neighbours | spoIID, ywmB |
| Gene sequence (+200bp) | Protein sequence |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
essential PubMed
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:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry: [3]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
MurAA is subject to ClpC-ClpP-dependent degradation PubMed
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
- Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
- Kock H, Gerth U, Hecker M. (2004) MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis. Mol Microbiol, 51:1087-1102. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
