Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis

FEMS Microbiol Lett. 2004 May 15;234(2):215-23. doi: 10.1016/j.femsle.2004.03.033.


Bacterial genomics have revealed the widespread occurrence of eukaryotic-like protein kinases in prokaryotes, but little is known about their regulation, endogenous substrates, and physiological role. The present study concerns one of these enzymes, the serine/threonine protein kinase PknF from Mycobacterium tuberculosis. It is shown that, in addition to its autokinase activity, PknF is able to phosphorylate Rv1747, a newly described ABC transporter. This reaction appears to involve two FHA domains of Rv1747. It is suggested that recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of PknF.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry*
  • ATP-Binding Cassette Transporters / genetics
  • ATP-Binding Cassette Transporters / metabolism*
  • Amino Acid Sequence
  • Amino Acid Substitution
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Binding Sites
  • DNA Primers
  • Genome, Bacterial
  • Genotype
  • Glutathione Transferase / metabolism
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Mycobacterium tuberculosis / enzymology*
  • Phosphorylation
  • Protein-Serine-Threonine Kinases / chemistry
  • Protein-Serine-Threonine Kinases / genetics
  • Protein-Serine-Threonine Kinases / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid


  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • DNA Primers
  • Recombinant Fusion Proteins
  • Rv1747 protein, Mycobacterium tuberculosis
  • Glutathione Transferase
  • PknF protein, Mycobacterium tuberculosis
  • Protein-Serine-Threonine Kinases