Difference between revisions of "MurAA"
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|style="background:#ABCDEF;" align="center"|'''Function''' || peptidoglycan precursor biosynthesis | |style="background:#ABCDEF;" align="center"|'''Function''' || peptidoglycan precursor biosynthesis | ||
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| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU36760 murAA] |
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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/cellwall.html Cell wall]''' | |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/cellwall.html Cell wall]''' | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[spoIID]]'', ''[[ywmB]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[spoIID]]'', ''[[ywmB]]'' | ||
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| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU36760 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU36760 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU36760 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:murAA_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:murAA_context.gif]] | ||
Revision as of 14:04, 13 May 2013
- Description: UDP-N-acetylglucosamine 1-carboxyvinyltransferase
| Gene name | murAA |
| Synonyms | murA |
| Essential | yes PubMed |
| Product | UDP-N-acetylglucosamine 1-carboxyvinyltransferase |
| Function | peptidoglycan precursor biosynthesis |
| Gene expression levels in SubtiExpress: murAA | |
| Metabolic function and regulation of this protein in SubtiPathways: Cell wall | |
| MW, pI | 46 kDa, 5.45 |
| Gene length, protein length | 1308 bp, 436 aa |
| Immediate neighbours | spoIID, ywmB |
| Sequences | Protein DNA Advanced_DNA |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
cell wall synthesis, biosynthesis of cell wall components, essential genes
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU36760
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: Phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine (according to Swiss-Prot)
- Protein family: MurA subfamily (according to Swiss-Prot)
- Paralogous protein(s): MurAB
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 3SG1 (from B. anthracis, 79% identity, 94% similarity)
- UniProt: P70965
- KEGG entry: [3]
- E.C. number: 2.5.1.7
Additional information
Expression and regulation
- 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
Jean van Heijenoort
Lipid intermediates in the biosynthesis of bacterial peptidoglycan.
Microbiol Mol Biol Rev: 2007, 71(4);620-35
[PubMed:18063720]
[WorldCat.org]
[DOI]
(P p)
Holger Kock, Ulf Gerth, Michael Hecker
MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis.
Mol Microbiol: 2004, 51(4);1087-102
[PubMed:14763982]
[WorldCat.org]
[DOI]
(P p)
