CysK

• Description: trigger enzyme: cysteine synthetase A and control of CymR activity
  
  

Gene name	cysK
Synonyms
Essential	no
Product	trigger enzyme: cysteine synthetase A
Function	biosynthesis of cysteine, control of CymR activity
Gene expression levels in SubtiExpress: cysK
Interactions involving this protein in SubtInteract: CysK
Metabolic function and regulation of this protein in SubtiPathways: Cys, Met & Sulfate assimilation
MW, pI	32 kDa, 5.492
Gene length, protein length	924 bp, 308 aa
Immediate neighbours	yacD, pabB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, transcription factors and their control, trigger enzyme

This gene is a member of the following regulons

CymR regulon, Spx regulon

The gene

Basic information

• Locus tag: BSU00730

Phenotypes of a mutant

constitutive expression of the cysH-cysP-sat-cysC-ylnD-ylnE-ylnF operon, auxotrophic for cysteine

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: O(3)-acetyl-L-serine + H₂S = L-cysteine + acetate (according to Swiss-Prot)

• Protein family: cysteine synthase/cystathionine beta-synthase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • CymR-CysK, the complex is formed in the presence of cysteine, and results in DNA binding and repression of genes of cysteine biosynthesis PubMed

• Localization:

Database entries

• Structure: 1Y7L (from Haemophilus influenzae, 39% identity, 52% similarity) PubMed

• UniProt: P37887

• KEGG entry: [3]

• E.C. number: 2.5.1.47

Expression and regulation

• Operon: cysK PubMed

• Expression browser: cysK PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by casamino acids PubMed
  • repressed in the presence of cysteine (CymR) PubMed

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

• Additional information:

Biological materials

• Mutant:
  • 1A834 ( cysK::kan), PubMed, available at BGSC
  • 1A801 ( cysK::spec), PubMed, available at BGSC
  • 1A803 ( cysK::spec), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Isabelle Martin-Verstraete, Institute Pasteur, Paris, France

References

Catherine Tanous, Olga Soutourina, Bertrand Raynal, Marie-Françoise Hullo, Peggy Mervelet, Anne-Marie Gilles, Philippe Noirot, Antoine Danchin, Patrick England, Isabelle Martin-Verstraete
The CymR regulator in complex with the enzyme CysK controls cysteine metabolism in Bacillus subtilis.
J Biol Chem: 2008, 283(51);35551-60
[PubMed:18974048] [WorldCat.org] [DOI] (P p)

Marie-Françoise Hullo, Sandrine Auger, Olga Soutourina, Octavian Barzu, Mireille Yvon, Antoine Danchin, Isabelle Martin-Verstraete
Conversion of methionine to cysteine in Bacillus subtilis and its regulation.
J Bacteriol: 2007, 189(1);187-97
[PubMed:17056751] [WorldCat.org] [DOI] (P p)

Sergine Even, Pierre Burguière, Sandrine Auger, Olga Soutourina, Antoine Danchin, Isabelle Martin-Verstraete
Global control of cysteine metabolism by CymR in Bacillus subtilis.
J Bacteriol: 2006, 188(6);2184-97
[PubMed:16513748] [WorldCat.org] [DOI] (P p)

Daniela Albanesi, Maria Cecilia Mansilla, Gustavo E Schujman, Diego de Mendoza
Bacillus subtilis cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation.
J Bacteriol: 2005, 187(22);7631-8
[PubMed:16267287] [WorldCat.org] [DOI] (P p)

Bin Huang, Matthew W Vetting, Steven L Roderick
The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase.
J Bacteriol: 2005, 187(9);3201-5
[PubMed:15838047] [WorldCat.org] [DOI] (P p)

Shunji Nakano, Michiko M Nakano, Ying Zhang, Montira Leelakriangsak, Peter Zuber
A regulatory protein that interferes with activator-stimulated transcription in bacteria.
Proc Natl Acad Sci U S A: 2003, 100(7);4233-8
[PubMed:12642660] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

J R van der Ploeg, M Barone, T Leisinger
Functional analysis of the Bacillus subtilis cysK and cysJI genes.
FEMS Microbiol Lett: 2001, 201(1);29-35
[PubMed:11445163] [WorldCat.org] [DOI] (P p)

Antoine de Saizieu, Pierre Vankan, Cassandra Vockler, Adolphus P G M van Loon
The trp RNA-binding attenuation protein (TRAP) regulates the steady-state levels of transcripts of the Bacillus subtilis folate operon.
Microbiology (Reading): 1997, 143 ( Pt 3);979-989
[PubMed:9084182] [WorldCat.org] [DOI] (P p)