DefB
- Description: N-formylcysteine deformylase, required for the conversion of S-methyl-cysteine to cysteine
Gene name | defB |
Synonyms | ykrB |
Essential | no |
Product | N-formylcysteine deformylase |
Function | utilization of S-methyl-cysteine |
Gene expression levels in SubtiExpress: defB | |
MW, pI | 20 kDa, 5.456 |
Gene length, protein length | 552 bp, 184 aa |
Immediate neighbours | ykrA, ykzV |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU14560
Phenotypes of a mutant
- no growth with S-methyl cysteine PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: N-acetylcysteine --> cysteine + acetate PubMed
- Protein family: polypeptide deformylase family (according to Swiss-Prot)
- Paralogous protein(s): DefA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure: 1LQY (complex with antibiotic actinonin, Geobacillus stearothermophilus)
- UniProt: Q45495
- KEGG entry: [2]
- E.C. number: 3.5.1.88
Additional information
Expression and regulation
- Operon:
- 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
Che-Man Chan, Antoine Danchin, Philippe Marlière, Agnieszka Sekowska
Paralogous metabolism: S-alkyl-cysteine degradation in Bacillus subtilis.
Environ Microbiol: 2014, 16(1);101-17
[PubMed:23944997]
[WorldCat.org]
[DOI]
(I 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)