DefA

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation, protein modification

The gene

Basic information

• Locus tag: BSU15720

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:
  • DefA-RplV PubMed
  • Map competes with peptide deformylase (DefA), the first enzyme to act on nascent chains, for binding sites at the ribosomal tunnel exit PubMed

• Localization:

Database entries

• Structure:

• UniProt: P94462

• KEGG entry: [2]

• E.C. number: 3.5.1.88

Expression and regulation

• Operon: defA-fmt-yloM PubMed

• Expression browser: defA PubMed

• Sigma factor: SigA defA-fmt-yloM PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Arzu Sandikci, Felix Gloge, Michael Martinez, Matthias P Mayer, Rebecca Wade, Bernd Bukau, Günter Kramer
Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding.
Nat Struct Mol Biol: 2013, 20(7);843-50
[PubMed:23770820] [WorldCat.org] [DOI] (I p)

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)