Difference between revisions of "DefA"

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(Basic information/ Evolution)
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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
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** [[DefA]]-[[RplV]] {{PubMed|18288106}}
  
 
* '''[[Localization]]:'''
 
* '''[[Localization]]:'''
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=References=
 
=References=
'''Additional publications:''' {{PubMed|16964327}}
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<pubmed>11429456,12627383, 18288106 16964327</pubmed>
<pubmed>11429456,12627383, </pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:24, 20 August 2013

  • Description: formylmethionine deformylase

Gene name defA
Synonyms yloK, def
Essential no
Product formylmethionine deformylase
Function translation
Gene expression levels in SubtiExpress: defA
MW, pI 17 kDa, 4.731
Gene length, protein length 480 bp, 160 aa
Immediate neighbours priA, fmt
Sequences Protein DNA DNA_with_flanks
Genetic context
Def context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Def expression.png















Categories containing this gene/protein

translation, protein modification

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU15720

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Formyl-L-methionyl peptide + H2O = formate + methionyl peptide (according to Swiss-Prot)
  • Protein family: polypeptide deformylase family (according to Swiss-Prot)
  • Paralogous protein(s): DefB

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • 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

Rouven Bingel-Erlenmeyer, Rebecca Kohler, Günter Kramer, Arzu Sandikci, Snjezana Antolić, Timm Maier, Christiane Schaffitzel, Brigitte Wiedmann, Bernd Bukau, Nenad Ban
A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing.
Nature: 2008, 452(7183);108-11
[PubMed:18288106] [WorldCat.org] [DOI] (I p)

Krzysztof Hinc, Adam Iwanicki, Simone Seror, Michał Obuchowski
Mapping of a transcription promoter located inside the priA gene of the Bacillus subtilis chromosome.
Acta Biochim Pol: 2006, 53(3);497-505
[PubMed:16964327] [WorldCat.org] (P p)

Julia Elisabeth Bandow, Dörte Becher, Knut Büttner, Falko Hochgräfe, Christoph Freiberg, Heike Brötz, Michael Hecker
The role of peptide deformylase in protein biosynthesis: a proteomic study.
Proteomics: 2003, 3(3);299-306
[PubMed:12627383] [WorldCat.org] [DOI] (P p)

Michael Haas, Dieter Beyer, Reinhold Gahlmann, Christoph Freiberg
YkrB is the main peptide deformylase in Bacillus subtilis, a eubacterium containing two functional peptide deformylases.
Microbiology (Reading): 2001, 147(Pt 7);1783-1791
[PubMed:11429456] [WorldCat.org] [DOI] (P p)