Difference between revisions of "CpgA"
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* '''Locus tag:''' BSU15780 | * '''Locus tag:''' BSU15780 | ||
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+ | [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=cpgA_1653103_1653999_1 Expression] | ||
===Phenotypes of a mutant === | ===Phenotypes of a mutant === |
Revision as of 09:19, 25 January 2012
- Description: GTPase, activity stimulated by ribosomes, may be involved in ribosome maturation
Gene name | cpgA |
Synonyms | yloQ |
Essential | no |
Product | GTPase |
Function | ribosome assembly, coordination of peptidoglycan deposition in the cell wall |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 33 kDa, 4.743 |
Gene length, protein length | 894 bp, 298 aa |
Immediate neighbours | prkC, rpe |
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
cell wall/ other, translation, GTP-binding proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15780
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: engC GTPase domain (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure: 1T9H
- UniProt: O34530
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Tony Wilkinson, York University, U.K. homepage
Your additional remarks
References
Reviews
Robert A Britton
Role of GTPases in bacterial ribosome assembly.
Annu Rev Microbiol: 2009, 63;155-76
[PubMed:19575570]
[WorldCat.org]
[DOI]
(I p)
Original publications