Fmt

• Description: methionyl-tRNA formyltransferase
  
  

Gene name	fmt
Synonyms	yloL
Essential	yes PubMed
Product	methionyl-tRNA formyltransferase
Function	formylation of Met-tRNA(fMet)
Gene expression levels in SubtiExpress: fmt
Metabolic function and regulation of this protein in SubtiPathways: fmt
MW, pI	34 kDa, 5.618
Gene length, protein length	951 bp, 317 aa
Immediate neighbours	defA, yloM
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation, essential genes

This gene is a member of the following regulons

Efp-dependent proteins

The gene

Basic information

• Locus tag: BSU15730

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU15730

• DBTBS entry: no entry

• SubtiList entry: [1]

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

• BsubCyc: BSU15730

• Structure: 3RFO (from Bacillus anthracis, 69% identity, 89% similarity)

• UniProt: P94463

• KEGG entry: [2]

• E.C. number: 2.1.2.9

Expression and regulation

• Operon: defA-fmt-yloM PubMed

• Expression browser: fmt PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • translation is likely to require Efp due to the presence of several consecutive proline residues PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)