Difference between revisions of "Fmt"

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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 951 bp, 317 aa  
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 951 bp, 317 aa  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[def]]'', ''[[yloM]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[defA]]'', ''[[yloM]]''
 
|-
 
|-
 
|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU15730 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU15730 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU15730 DNA_with_flanks]
 
|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU15730 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU15730 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU15730 DNA_with_flanks]
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=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:''' ''[[def]]-[[fmt]]-[[yloM]]'' [http://www.ncbi.nlm.nih.gov/pubmed/16964327?ordinalpos=5&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum PubMed]
+
* '''Operon:''' ''[[defA]]-[[fmt]]-[[yloM]]'' {{PubMed|16964327}}
  
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=fmt_1646999_1647952_1 fmt] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=fmt_1646999_1647952_1 fmt] {{PubMed|22383849}}
  
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/pubmed/16964327?ordinalpos=5&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum PubMed]
+
* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|16964327}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  

Revision as of 11:00, 18 August 2013

  • 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:
tRNA charging
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
Fmt context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Fmt expression.png















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

  • 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:

Database entries

  • Structure: 3RFO (from Bacillus anthracis, 69% identity, 89% similarity)
  • KEGG entry: [2]

Additional information

Expression and regulation

  • 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:

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)