Difference between revisions of "TkmA"

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(Categories containing this gene/protein)
(References)
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'''Additional publications:''' {{PubMed|20817675}}
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<pubmed>12970183, 20815827 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:48, 24 April 2011

  • Description: transmembrane modulator of PtkA activity, activates PtkA autophosphorylation and substrate phosphorylation

Gene name tkmA
Synonyms ywqC
Essential no
Product modulator of PtkA activity
Function control of protein tyrosine phosphorylation
MW, pI 26 kDa, 4.61
Gene length, protein length 744 bp, 248 aa
Immediate neighbours ptkA, ywqB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YwqC context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

biofilm formation, protein modification, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU36260

Phenotypes of a mutant

the mutant exhibits a defect in biofilm formation PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: transmembrane activation of PtkA protein tyrosine kinase activity
  • Protein family: cpsC/capA family (according to Swiss-Prot)
  • Paralogous protein(s): EpsA

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Taryn B Kiley, Nicola R Stanley-Wall
Post-translational control of Bacillus subtilis biofilm formation mediated by tyrosine phosphorylation.
Mol Microbiol: 2010, 78(4);947-63
[PubMed:20815827] [WorldCat.org] [DOI] (I p)

Ivan Mijakovic, Sandrine Poncet, Grégory Boël, Alain Mazé, Sylvie Gillet, Emmanuel Jamet, Paulette Decottignies, Christophe Grangeasse, Patricia Doublet, Pierre Le Maréchal, Josef Deutscher
Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases.
EMBO J: 2003, 22(18);4709-18
[PubMed:12970183] [WorldCat.org] [DOI] (P p)