PtkA

• Description: protein tyrosine kinase
  
  

Gene name	ptkA
Synonyms	ywqD
Essential	no
Product	protein tyrosine kinase
Function	protein phosphorylation
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

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

• 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

• 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

• 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

• 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)

Original publications

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)

Boumediene Soufi, Chanchal Kumar, Florian Gnad, Matthias Mann, Ivan Mijakovic, Boris Macek
Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
J Proteome Res: 2010, 9(7);3638-46
[PubMed:20509597] [WorldCat.org] [DOI] (I p)

Carsten Jers, Malene Mejer Pedersen, Dafni Katerina Paspaliari, Wolfgang Schütz, Christina Johnsson, Boumediene Soufi, Boris Macek, Peter Ruhdal Jensen, Ivan Mijakovic
Bacillus subtilis BY-kinase PtkA controls enzyme activity and localization of its protein substrates.
Mol Microbiol: 2010, 77(2);287-99
[PubMed:20497499] [WorldCat.org] [DOI] (I p)

Dina Petranovic, Christophe Grangeasse, Boris Macek, Mohammad Abdillatef, Virginie Gueguen-Chaignon, Sylvie Nessler, Josef Deutscher, Ivan Mijakovic
Activation of Bacillus subtilis Ugd by the BY-kinase PtkA proceeds via phosphorylation of its residue tyrosine 70.
J Mol Microbiol Biotechnol: 2009, 17(2);83-9
[PubMed:19258708] [WorldCat.org] [DOI] (I p)

Vanesa Olivares-Illana, Philippe Meyer, Emmanuelle Bechet, Virginie Gueguen-Chaignon, Didier Soulat, Sylvie Lazereg-Riquier, Ivan Mijakovic, Josef Deutscher, Alain J Cozzone, Olivier Laprévote, Solange Morera, Christophe Grangeasse, Sylvie Nessler
Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus.
PLoS Biol: 2008, 6(6);e143
[PubMed:18547145] [WorldCat.org] [DOI] (I p)

Dina Petranovic, Ole Michelsen, Ksenija Zahradka, Catarina Silva, Mirjana Petranovic, Peter Ruhdal Jensen, Ivan Mijakovic
Bacillus subtilis strain deficient for the protein-tyrosine kinase PtkA exhibits impaired DNA replication.
Mol Microbiol: 2007, 63(6);1797-805
[PubMed:17367396] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Lucia Musumeci, Lutz Tautz, Dina Petranovic, Robert A Edwards, Peter Ruhdal Jensen, Tomas Mustelin, Josef Deutscher, Nunzio Bottini
In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE.
J Bacteriol: 2005, 187(10);3384-90
[PubMed:15866923] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Dina Petranovic, Josef Deutscher
How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF.
J Mol Microbiol Biotechnol: 2004, 8(1);19-25
[PubMed:15741737] [WorldCat.org] [DOI] (P 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)