Difference between revisions of "GatB"
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| − | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=gatB_730509_731939_1 gatB] {{PubMed|22383849}} |
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=Biological materials = | =Biological materials = | ||
Revision as of 15:38, 12 April 2012
- Description: production of glutamyl-tRNA(Gln)
| Gene name | gatB |
| Synonyms | yerN |
| Essential | yes PubMed |
| Product | glutamyl-tRNA(Gln) amidotransferase (sununit B) |
| Function | translation |
| Interactions involving this protein in SubtInteract: GatB | |
| Metabolic function and regulation of this protein in SubtiPathways: tRNA charging | |
| MW, pI | 53 kDa, 4.898 |
| Gene length, protein length | 1428 bp, 476 aa |
| Immediate neighbours | gatA, yerO |
| 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: BSU06690
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate (according to Swiss-Prot)
- Protein family: GatB subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: O30509
- KEGG entry: [2]
- 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
Takuhiro Ito, Shigeyuki Yokoyama
Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions.
Nature: 2010, 467(7315);612-6
[PubMed:20882017]
[WorldCat.org]
[DOI]
(I p)
A W Curnow, K w Hong, R Yuan, S i Kim, O Martins, W Winkler, T M Henkin, D Söll
Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation.
Proc Natl Acad Sci U S A: 1997, 94(22);11819-26
[PubMed:9342321]
[WorldCat.org]
[DOI]
(P p)
