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  • 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
Gene expression levels in SubtiExpress: tkmA
Interactions involving this protein in SubtInteract: TkmA
MW, pI 26 kDa, 4.61
Gene length, protein length 744 bp, 248 aa
Immediate neighbours ptkA, ywzD
Sequences Protein DNA DNA_with_flanks
Genetic context
YwqC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TkmA expression.png

Categories containing this gene/protein

biofilm formation, protein modification, membrane proteins

This gene is a member of the following regulons

AbrB regulon

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:

Database entries

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

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
    • GP1566 (spc), available in Stülke lab;
    • GP1567 epsA::aphA3 tkmA::spc, available in Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks


Abderahmane Derouiche, Vladimir Bidnenko, Rosa Grenha, Nathalie Pigonneau, Magali Ventroux, Mirita Franz-Wachtel, Sylvie Nessler, Marie-Françoise Noirot-Gros, Ivan Mijakovic
Interaction of bacterial fatty-acid-displaced regulators with DNA is interrupted by tyrosine phosphorylation in the helix-turn-helix domain.
Nucleic Acids Res.: 2013, 41(20);9371-81
[PubMed:23939619] [] [DOI] (I p)

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res.: 2011, 39(2);414-28
[PubMed:20817675] [] [DOI] (I p)

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] [] [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] [] [DOI] (P p)