Gmk

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  • Description: guanylate kinase (GMP:dATP, dGMP:ATP)

Gene name gmk
Synonyms yloD
Essential yes PubMed
Product guanylate kinase (GMP:dATP, dGMP:ATP)
Function GTP biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Purine salvage, Nucleotides (regulation)
MW, pI 23 kDa, 4.616
Gene length, protein length 612 bp, 204 aa
Immediate neighbours ylzA, yloH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Gmk context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Gmk expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, essential genes, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU15680

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 + GMP = ADP + GDP (according to Swiss-Prot)
  • Protein family: guanylate kinase-like domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylated on Arg-134 and/or Arg-149PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1S4Q (from Mycobacterium tuberculosis h37rv, 39% identity, 60% similarity)
  • 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

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)