TkmA

• 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
Interactions involving this protein in SubtInteract: TkmA
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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]

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:

• Interactions:
  • PtkA-TkmA PubMed

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: P96715

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: tkmA-ptkA-ptpZ-ugd PubMed

• Expression browser: tkmA PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:
  • DegU-P: transcription repression PubMed
  • AbrB: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)