Difference between revisions of "DefA"
| Line 87: | Line 87: | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
** [[DefA]]-[[RplV]] {{PubMed|18288106}} | ** [[DefA]]-[[RplV]] {{PubMed|18288106}} | ||
| + | ** [[Map]] competes with peptide deformylase ([[DefA]]), the first enzyme to act on nascent chains, for binding sites at the ribosomal tunnel exit {{PubMed|23770820}} | ||
* '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
| Line 135: | Line 136: | ||
=References= | =References= | ||
| − | <pubmed>11429456,12627383, 18288106 16964327</pubmed> | + | <pubmed>11429456,12627383, 18288106 16964327 23770820</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 12:29, 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 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
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:
- UniProt: P94462
- KEGG entry: [2]
- E.C. number: 3.5.1.88
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
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)
