Difference between revisions of "YjdI"
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=Biological materials = | =Biological materials = |
Revision as of 18:07, 12 April 2012
- Description: similiar to Cys-tRNA(Pro) and Cys-tRNA(Cys) deacylase
Gene name | yjdI |
Synonyms | |
Essential | no |
Product | Cys-tRNA(Pro) and Cys-tRNA(Cys) deacylase |
Function | maturation of tRNA |
MW, pI | 17 kDa, 8.755 |
Gene length, protein length | 477 bp, 159 aa |
Immediate neighbours | yjdH, yjdJ |
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: BSU12060
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
E. coli homolog: [2]
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:
- Localization:
Database entries
- Structure:
- UniProt: O31650
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Songon An, Karin Musier-Forsyth
Cys-tRNA(Pro) editing by Haemophilus influenzae YbaK via a novel synthetase.YbaK.tRNA ternary complex.
J Biol Chem: 2005, 280(41);34465-72
[PubMed:16087664]
[WorldCat.org]
[DOI]
(P p)
Benfang Ruan, Dieter Söll
The bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys deacylase.
J Biol Chem: 2005, 280(27);25887-91
[PubMed:15886196]
[WorldCat.org]
[DOI]
(P p)
Fai-Chu Wong, Penny J Beuning, Carmen Silvers, Karin Musier-Forsyth
An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing.
J Biol Chem: 2003, 278(52);52857-64
[PubMed:14530268]
[WorldCat.org]
[DOI]
(P p)