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: cysK
MW, pI	32 kDa, 5.492
Gene length, protein length	924 bp, 308 aa
Immediate neighbours	yacD, pabB
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

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

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

• BsubCyc: BSU00730

• 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:

• Cofactors:

• 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

• BsubCyc: BSU00730

• 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:
  • belongs to the 100 most abundant proteins PubMed

Biological materials

• Mutant:
  • 1A834 ( cysK::kan), PubMed, available at BGSC
  • 1A801 ( cysK::spec), PubMed, available at BGSC
  • 1A803 ( cysK::spec), PubMed, available at BGSC
  • 1A946 ( 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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)