Difference between revisions of "Fmt"
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− | * '''Structure:''' [http://www. | + | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=3RFO 3RFO] (from ''Bacillus anthracis'', 69% identity, 89% similarity) |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P94463 P94463] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P94463 P94463] |
Revision as of 19:49, 27 April 2011
- Description: methionyl-tRNA formyltransferase
Gene name | fmt |
Synonyms | yloL |
Essential | yes PubMed |
Product | methionyl-tRNA formyltransferase |
Function | formylation of Met-tRNA(fMet) |
Metabolic function and regulation of this protein in SubtiPathways: tRNA charging | |
MW, pI | 34 kDa, 5.618 |
Gene length, protein length | 951 bp, 317 aa |
Immediate neighbours | def, yloM |
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: BSU15730
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: 10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) + H2O = tetrahydrofolate + N-formylmethionyl-tRNA(fMet) (according to Swiss-Prot)
- Protein family: fmt family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 3RFO (from Bacillus anthracis, 69% identity, 89% similarity)
- UniProt: P94463
- KEGG entry: [2]
- E.C. number: 2.1.2.9
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
Your additional remarks
References
Additional references: PubMed
Yann Duroc, Carmela Giglione, Thierry Meinnel
Mutations in three distinct loci cause resistance to peptide deformylase inhibitors in Bacillus subtilis.
Antimicrob Agents Chemother: 2009, 53(4);1673-8
[PubMed:19171795]
[WorldCat.org]
[DOI]
(I p)