Difference between revisions of "PbpA"
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=== Additional information=== | === Additional information=== | ||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
+ | ** part of the [[cell wall biosynthetic complex]] {{PubMed|21636744,21636745}} | ||
** folding requires [[PrsA]] {{PubMed|20487272}} | ** folding requires [[PrsA]] {{PubMed|20487272}} | ||
Revision as of 05:18, 11 July 2011
- 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 |
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
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
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