Difference between revisions of "Fmt"

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(References)
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=References=
 
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'''Additional references:''' {{PubMed|16964327}}
 
'''Additional references:''' {{PubMed|16964327}}
<pubmed>,19171795</pubmed>
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<pubmed>8887566,19171795</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

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
Fmt context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

translation, essential genes

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)
  • KEGG entry: [2]

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)

E Schmitt, S Blanquet, Y Mechulam
Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase.
EMBO J: 1996, 15(17);4749-58
[PubMed:8887566] [WorldCat.org] (P p)