Difference between revisions of "CpgA"
(→Original publications) |
(→Original publications) |
||
Line 126: | Line 126: | ||
<pubmed> 19575570 </pubmed> | <pubmed> 19575570 </pubmed> | ||
==Original publications== | ==Original publications== | ||
− | + | ||
− | <pubmed>15223319,16485133,14747714,16025310,18344364,19246764,19246764,15828870,17005971,18344364,18984160 </pubmed> | + | <pubmed> 15223319, 16485133, 14747714, 16025310, 18344364, 19246764, 19246764, 15828870, 17005971, 18344364, 18984160 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 09:58, 18 June 2010
- 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
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:
- Interactions:
- Localization:
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
Original publications