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

• 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
  • FatR-PtkA 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; GP1520 (spc), GP1544 (ermC) and GP1587 (cat) , available in Stülke lab; GP1521 epsB (aphA3) ptkA (spc) double mutant available in Stülke lab; GP1529 tkmA-ptkA::spc available in Stülke 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:

• 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

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)

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)