Difference between revisions of "CysK"
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===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
| − | |||
constitutive expression of the ''[[cysH]]-[[cysP]]-[[sat]]-[[cysC]]-[[ylnD]]-[[ylnE]]-[[ylnF]]'' operon, auxotrophic for cysteine | constitutive expression of the ''[[cysH]]-[[cysP]]-[[sat]]-[[cysC]]-[[ylnD]]-[[ylnE]]-[[ylnF]]'' operon, auxotrophic for cysteine | ||
| Line 84: | Line 83: | ||
* '''Effectors of protein activity:''' | * '''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 [http://www.ncbi.nlm.nih.gov/sites/entrez/18974048 PubMed] | + | * '''Interactions:''' |
| + | ** [[CymR]]-[[CysK]], the complex is formed in the presence of cysteine, and results in DNA binding and repression of genes of cysteine biosynthesis [http://www.ncbi.nlm.nih.gov/sites/entrez/18974048 PubMed] | ||
* '''Localization:''' | * '''Localization:''' | ||
| Line 138: | Line 138: | ||
=References= | =References= | ||
| − | <pubmed>16513748,17056751,18974048,16267287, 12642660,11445163 ,12107147 , </pubmed> | + | <pubmed>16513748,17056751,18974048,16267287, 12642660,11445163 ,12107147 ,15838047 9084182 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 18:30, 16 April 2011
- 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 |
| 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
| |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, trigger enzyme
This gene is a member of the following regulons
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]
Additional information
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:
- Localization:
Database entries
- UniProt: P37887
- KEGG entry: [3]
- E.C. number: 2.5.1.47
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Isabelle Martin-Verstraete, Institute Pasteur, Paris, France
Your additional remarks
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)
