PtkA

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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
YwqD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PtkA expression.png















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]

Additional information

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
  • 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

Database entries

  • Structure: 2VED (CapB, the homolog in Staphylococcus aureus)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • 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
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Ivan Mijakovic, Thiverval-Grignon, France

Your additional remarks

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)