Difference between revisions of "PtkA"

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* '''Catalyzed reaction/ biological activity:'''  
 
* '''Catalyzed reaction/ biological activity:'''  
  
* '''Protein family:'''
+
* '''Protein family:''' BY-kinase
  
 
* '''Paralogous protein(s):'''
 
* '''Paralogous protein(s):'''
Line 64: Line 64:
 
* '''Domains:'''  
 
* '''Domains:'''  
  
* '''Modification:'''
+
* '''Modification:''' autophosphorylation at residues Y225, Y227 and Y228 (primary site)
  
* '''Cofactor(s):'''
+
* '''Cofactor(s):''' ATP
  
* '''Effectors of protein activity:'''
+
* '''Effectors of protein activity:''' TkmA - transmembrane modulator, activates PtkA autophosphorylation and substrate phosphorylation
  
 
* '''Interactions:'''
 
* '''Interactions:'''
Line 100: Line 100:
 
=Biological materials =
 
=Biological materials =
  
* '''Mutant:'''
+
* '''Mutant:''' KO strain created with pMUTIN-2
  
* '''Expression vector:'''
+
* '''Expression vector:''' pQE-30, N-terminally 6xHis-tagged
 
          
 
          
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''
Line 112: Line 112:
 
* '''Antibody:'''
 
* '''Antibody:'''
  
=Labs working on this gene/protein=
+
=Labs working on this gene/protein= Ivan Mijakovic
  
 
=Your additional remarks=
 
=Your additional remarks=
Line 119: Line 119:
  
 
# Mijakovic I, Poncet S, Boël G, Mazé A, Gillet S, Decottignies P, Grangeasse C, Jamet E, Doublet P, Le Maréchal P, Deutscher J (2003) Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases. EMBO J  22:4709-4718.  [http://www.ncbi.nlm.nih.gov/sites/entrez/12970183 PubMed]
 
# Mijakovic I, Poncet S, Boël G, Mazé A, Gillet S, Decottignies P, Grangeasse C, Jamet E, Doublet P, Le Maréchal P, Deutscher J (2003) Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases. EMBO J  22:4709-4718.  [http://www.ncbi.nlm.nih.gov/sites/entrez/12970183 PubMed]
# Mijakovic I, Petranovic D, Macek B, Cepo T, Mann M, Davies J, Jensen PR, Vujaklija D: Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine. Nucl Acids Res 2006, 34:1588-1596.  [http://www.ncbi.nlm.nih.gov/sites/entrez/16549871 PubMed]
+
# Mijakovic I, Petranovic D, Deutscher J (2004) How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF. J Mol Microbiol Biotechnol 8:19-25.  [http://www.ncbi.nlm.nih.gov/sites/entrez/15741737 PubMed]
 +
# Mijakovic I, Petranovic D, Macek B, Cepo T, Mann M, Davies J, Jensen PR, Vujaklija D (2006) Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine. Nucl Acids Res 34:1588-1596.  [http://www.ncbi.nlm.nih.gov/sites/entrez/16549871 PubMed]
 +
# Petranovic D, Michelsen O, Zahradka K, Silva C, Petranovic M, Jensen PR, Mijakovic I (2007) Bacillus subtilis strain deficient for the protein-tyrosine kinase PtkA exhibits impaired DNA replication. Mol Microbiol 63:1797-1805. [http://www.ncbi.nlm.nih.gov/sites/entrez/17367396 PubMed]
 +
 
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 11:20, 15 March 2009

  • Description: write here

Gene name ptkA
Synonyms ywqD
Essential no
Product
Function unknown
MW, pI 25 kDa, 9.628
Gene length, protein length 711 bp, 237 aa
Immediate neighbours ptpZ, tkmA
Gene sequence (+200bp) Protein sequence
Genetic context
YwqD context.gif



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: BY-kinase
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: autophosphorylation at residues Y225, Y227 and Y228 (primary site)
  • Cofactor(s): ATP
  • Effectors of protein activity: TkmA - transmembrane modulator, activates PtkA autophosphorylation and substrate phosphorylation
  • Interactions:
  • Localization:

Database entries

  • Structure:
  • Swiss prot entry:
  • KEGG entry:
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: KO strain created with pMUTIN-2
  • Expression vector: pQE-30, N-terminally 6xHis-tagged
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

=Labs working on this gene/protein= Ivan Mijakovic

Your additional remarks

References

  1. Mijakovic I, Poncet S, Boël G, Mazé A, Gillet S, Decottignies P, Grangeasse C, Jamet E, Doublet P, Le Maréchal P, Deutscher J (2003) Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases. EMBO J 22:4709-4718. PubMed
  2. Mijakovic I, Petranovic D, Deutscher J (2004) How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF. J Mol Microbiol Biotechnol 8:19-25. PubMed
  3. Mijakovic I, Petranovic D, Macek B, Cepo T, Mann M, Davies J, Jensen PR, Vujaklija D (2006) Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine. Nucl Acids Res 34:1588-1596. PubMed
  4. Petranovic D, Michelsen O, Zahradka K, Silva C, Petranovic M, Jensen PR, Mijakovic I (2007) Bacillus subtilis strain deficient for the protein-tyrosine kinase PtkA exhibits impaired DNA replication. Mol Microbiol 63:1797-1805. PubMed
  1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed