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
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 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, pronounced on LBGM medium, weak of MSgg medium PubMed

Database entries

• BsubCyc: BSU36260

• 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, TkmA can partially replace EpsA PubMed

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • PtkA-TkmA PubMed
  • FatR-TkmA PubMed

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

Database entries

• BsubCyc: BSU36260

• 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:
  • GP1566 (spc) PubMed, available in Jörg Stülke's lab
  • GP1567 epsA::aphA3 tkmA::spc PubMed, available in Jörg Stülke's lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

• FLAG-tag construct: GP1620 tkmA-FLAG 3x spc (based on pGP1331) available in Jörg Stülke's lab

• Antibody:

References

Tantan Gao, Jennifer Greenwich, Yan Li, Qi Wang, Yunrong Chai
The Bacterial Tyrosine Kinase Activator TkmA Contributes to Biofilm Formation Largely Independently of the Cognate Kinase PtkA in Bacillus subtilis.
J Bacteriol: 2015, 197(21);3421-32
[PubMed:26283769] [WorldCat.org] [DOI] (I p)

Jan Gerwig, Taryn B Kiley, Katrin Gunka, Nicola Stanley-Wall, Jörg Stülke
The protein tyrosine kinases EpsB and PtkA differentially affect biofilm formation in Bacillus subtilis.
Microbiology (Reading): 2014, 160(Pt 4);682-691
[PubMed:24493247] [WorldCat.org] [DOI] (I p)

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] [WorldCat.org] [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] [WorldCat.org] [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] [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)