PtkA

• Description: protein tyrosine kinase
  
  

Gene name	ptkA
Synonyms	ywqD
Essential	no
Product	protein tyrosine kinase
Function	protein phosphorylation
Gene expression levels in SubtiExpress: ptkA
Interactions involving this protein in SubtInteract: PtkA
MW, pI	25 kDa, 9.628
Gene length, protein length	711 bp, 237 aa
Immediate neighbours	ptpZ, tkmA
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: BSU36250

Phenotypes of a mutant

• Accumulation of extra chromosome equivalents PubMed
• Defect in biofilm formation, this involves the kinase activity, but the target protein is unknown PubMed

Database entries

• BsubCyc: BSU36250

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate (according to Swiss-Prot), autophosphorylation, phosphorylation of Ugd, TuaD, Ssb, SsbB

• Protein family: BY-kinase, see the Bacterial Protein Tyrosine Kinase Database)

• Paralogous protein(s): EpsB

Extended information on the protein

• Kinetic information:

• Domains: single BY-kinase domain

• Modification: autophosphorylation at residues Y225, Y227 and Y228 (primary site) PubMed, dephosphorylated by PtpZ PubMed

• Cofactors: ATP

• Effectors of protein activity: TkmA - transmembrane modulator, activates PtkA autophosphorylation and substrate phosphorylation PubMed

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

• Localization:

Database entries

• BsubCyc: BSU36250

• Structure: 2VED (CapB, the homolog in Staphylococcus aureus)

• UniProt: P96716

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: tkmA-ptkA-ptpZ-ugd PubMed

• Expression browser: ptkA PubMed

• Sigma factor: SigA PubMed

• Regulation:

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

• Additional information:

Biological materials

• Mutant:
  • KO strain created with pMUTIN-2, available from Ivan Mijakovic
  • GP1520 (spc), available in Jörg Stülke's lab
  • GP1544 (ermC), available in Jörg Stülke's lab
  • GP1587 (cat) , available in Jörg Stülke's lab
  • GP1521 epsB (aphA3) ptkA (spc) double mutant available in Jörg Stülke's lab
  • GP1529 tkmA-ptkA::spc available in Jörg Stülke's lab
  • GP1610 (ptkA-ptpZ, spc), available in Jörg Stülke's lab

• Expression vector: pQE-30, N-terminally 6xHis-tagged, available from Ivan Mijakovic

• lacZ fusion: in a KO strain created with pMUTIN-2, available from Ivan Mijakovic

• GFP fusion: CFP-fusion, available from Ivan Mijakovic

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

• Antibody:

Labs working on this gene/protein

Ivan Mijakovic, Thiverval-Grignon, France

References

Reviews

Ivan Mijakovic, Josef Deutscher
Protein-tyrosine phosphorylation in Bacillus subtilis: a 10-year retrospective.
Front Microbiol: 2015, 6;18
[PubMed:25667587] [WorldCat.org] [DOI] (P e)

Jan Gerwig, Jörg Stülke
Far from being well understood: multiple protein phosphorylation events control cell differentiation in Bacillus subtilis at different levels.
Front Microbiol: 2014, 5;704
[PubMed:25540643] [WorldCat.org] [DOI] (P e)

Joseph D Chao, Dennis Wong, Yossef Av-Gay
Microbial protein-tyrosine kinases.
J Biol Chem: 2014, 289(14);9463-72
[PubMed:24554699] [WorldCat.org] [DOI] (I p)

Jörg Stülke
More than just activity control: phosphorylation may control all aspects of a protein's properties.
Mol Microbiol: 2010, 77(2);273-5
[PubMed:20497498] [WorldCat.org] [DOI] (I p)