Difference between revisions of "PtkA"
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==Original publications== | ==Original publications== | ||
<pubmed> 12970183, 15741737, 15866923, 17367396, 19258708 18547145 20497499 20509597 20815827 20817675 23939619 24493247 24728941 </pubmed> | <pubmed> 12970183, 15741737, 15866923, 17367396, 19258708 18547145 20497499 20509597 20815827 20817675 23939619 24493247 24728941 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 13:52, 28 May 2014
- 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 |
Contents
Categories containing this gene/protein
biofilm formation, protein modification, membrane proteins
This gene is a member of the following regulons
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]
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
- 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
Database entries
- BsubCyc: BSU36250
- Structure: 2VED (CapB, the homolog in Staphylococcus aureus)
- UniProt: P96716
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- 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
Your additional remarks
References
Reviews
Original publications
Lei Shi, Boyang Ji, Lorena Kolar-Znika, Ana Boskovic, Fanny Jadeau, Christophe Combet, Christophe Grangeasse, Damjan Franjevic, Emmanuel Talla, Ivan Mijakovic
Evolution of bacterial protein-tyrosine kinases and their relaxed specificity toward substrates.
Genome Biol Evol: 2014, 6(4);800-17
[PubMed:24728941]
[WorldCat.org]
[DOI]
(I p)
Jan Gerwig, Taryn B Kiley, Katrin Gunka, Nicola Stanley-Wall, Jörg Stülke
The protein tyrosine kinases EpsB and PtkA differentially affect biofilm formation in Bacillus subtilis.
Microbiology (Reading): 2014, 160(Pt 4);682-691
[PubMed:24493247]
[WorldCat.org]
[DOI]
(I p)
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)