Difference between revisions of "Tmk"

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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=tmk_39159_39797_1 tmk] {{PubMed|22383849}}
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=Biological materials =
 
=Biological materials =

Revision as of 14:50, 7 August 2012

  • Description: thymidylate kinase

Gene name tmk
Synonyms yaaP
Essential yes PubMed
Product thymidylate kinase
Function TTP biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Nucleotides (regulation)
MW, pI 23 kDa, 4.866
Gene length, protein length 636 bp, 212 aa
Immediate neighbours yaaO, yaaQ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Tmk context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU00280

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + dTMP = ADP + dTDP (according to Swiss-Prot)
  • Protein family: thymidylate kinase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2CCK (from Staphylococcus aureus, 53% identity, 74% similarity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Masayo Kotaka, Balvinder Dhaliwal, Jingshan Ren, Charles E Nichols, Richard Angell, Michael Lockyer, Alastair R Hawkins, David K Stammers
Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding.
Protein Sci: 2006, 15(4);774-84
[PubMed:16522804] [WorldCat.org] [DOI] (P p)