Difference between revisions of "PtkA"

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(Biological materials)
(Biological materials)
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=Biological materials =
 
=Biological materials =
  
* '''Mutant:''' KO strain created with pMUTIN-2, available from [[Ivan Mijakovic]]; GP1520 (spc), available in [[Stülke]] lab; GP1521 epsB (aphA3) ptkA (spc) double mutant available in [[Stülke]] lab; GP1529 tkmA-ptkA::spc available in [[Stülke]] lab
+
* '''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]]
 
* '''Expression vector:''' pQE-30, N-terminally 6xHis-tagged, available from [[Ivan Mijakovic]]

Revision as of 16:59, 27 January 2014

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