Difference between revisions of "PbpA"
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* '''Operon:''' ''[[pbpA]]'' {{PubMed|21815947}} | * '''Operon:''' ''[[pbpA]]'' {{PubMed|21815947}} | ||
− | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pbpA_2581771_2583921_-1 pbpA] {{PubMed|22383849}} |
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+ | * '''Sigma factor:''' | ||
* '''Regulation:''' | * '''Regulation:''' |
Revision as of 11:23, 16 April 2012
- Description: penicillin-binding protein PBP 2A
Gene name | pbpA |
Synonyms | yqgF |
Essential | no |
Product | penicillin-binding protein PBP 2A |
Function | formation of a rod-shaped peptidoglycan cell wall, spore outgrowth |
Interactions involving this protein in SubtInteract: PbpA | |
MW, pI | 79 kDa, 9.571 |
Gene length, protein length | 2148 bp, 716 aa |
Immediate neighbours | pstS, yqgE |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU25000
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
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:
- part of the cell wall biosynthetic complex PubMed
- folding requires PrsA PubMed
- Localization: extracellular (signal peptide) PubMed
Database entries
- Structure:
- UniProt: P54488
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- Regulatory mechanism:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jeff Errington lab
- Antibody:
Labs working on this gene/protein
Jeff Errington, Newcastle University, UK homepage
Your additional remarks
References
Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol Microbiol. 2011 81(6): 1459-1473. PubMed:21815947