PtkA

• Description: protein tyrosine kinase
  
  

Gene name	ptkA
Synonyms	ywqD
Essential	no
Product	protein tyrosine kinase
Function	protein phosphorylation
MW, pI	25 kDa, 9.628
Gene length, protein length	711 bp, 237 aa
Immediate neighbours	ptpZ, tkmA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU36250

Phenotypes of a mutant

Accumulation of extra chromosome equivalents PubMed

Database entries

• 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: cpsD/capB family (according to Swiss-Prot), BY-kinase

• 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), dephosphorylated by PtpZ PubMed

• Cofactor(s): ATP

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

• Interactions: PtkA-TkmA PubMed

• Localization:

Database entries

• 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

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: KO strain created with pMUTIN-2, available from Ivan Mijakovic

• 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:

• Antibody:

Labs working on this gene/protein

Ivan Mijakovic, Thiverval-Grignon, France

References

Reviews

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)