SnaA

• Description: sulphur N-acetylase, required for the conversion of S-methyl-cysteine to cysteine
  
  

Gene name	ytmI
Synonyms
Essential	no
Product	sulphur N-acetylase
Function	utilization of S-methyl-cysteine
Gene expression levels in SubtiExpress: snaA
Metabolic function and regulation of this protein in SubtiPathways: Riboflavin / FAD
MW, pI	20 kDa, 5.508
Gene length, protein length	534 bp, 178 aa
Immediate neighbours	tcyJ, ascR
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

sulfur metabolism

This gene is a member of the following regulons

CymR regulon, AscR regulon

The gene

Basic information

• Locus tag: BSU29390

Phenotypes of a mutant

• reduced growth with S-methyl cysteine PubMed
• the snaA snaB double mutant does not grow with S-methyl cysteine PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • N-acetylation of the amino group of S-methyl cysteine PubMed

• Protein family: acetyltransferase family (according to Swiss-Prot)

• Paralogous protein(s): SnaB

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: O34350

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: snaA-tcyJ-tcyK-tcyL-tcyM-tcyN-cmoO-cmoI-cmoJ-ribR-sndA-ytnM PubMed

• Expression browser: snaA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed in the presence of cysteine (CymR) PubMed
  • induced in the presence of S-methyl-cysteine (AscR) PubMed

• Regulatory mechanism:
  • CymR: transcription repression PubMed
  • AscR: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

Pierre Burguière, Juliette Fert, Isabelle Guillouard, Sandrine Auger, Antoine Danchin, Isabelle Martin-Verstraete
Regulation of the Bacillus subtilis ytmI operon, involved in sulfur metabolism.
J Bacteriol: 2005, 187(17);6019-30
[PubMed:16109943] [WorldCat.org] [DOI] (P p)

Kyle N Erwin, Shunji Nakano, Peter Zuber
Sulfate-dependent repression of genes that function in organosulfur metabolism in Bacillus subtilis requires Spx.
J Bacteriol: 2005, 187(12);4042-9
[PubMed:15937167] [WorldCat.org] [DOI] (P p)

Irina M Solovieva, Rimma A Kreneva, Lubov Errais Lopes, Daniel A Perumov
The riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product.
FEMS Microbiol Lett: 2005, 243(1);51-8
[PubMed:15668000] [WorldCat.org] [DOI] (P p)

Jean-Yves Coppée, Sandrine Auger, Evelyne Turlin, Agnieszka Sekowska, Jean-Pierre Le Caer, Valérie Labas, Valérie Vagner, Antoine Danchin, Isabelle Martin-Verstraete
Sulfur-limitation-regulated proteins in Bacillus subtilis: a two-dimensional gel electrophoresis study.
Microbiology (Reading): 2001, 147(Pt 6);1631-1640
[PubMed:11390694] [WorldCat.org] [DOI] (P p)