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A new family of bacterial regulatory proteins

David J. Haydon, John R. Guest
DOI: http://dx.doi.org/10.1111/j.1574-6968.1991.tb04544.x 291-295 First published online: 1 April 1991


A new family of bacterial regulatory proteins has been identified by sequence similarity. The family contains the repressor of the Bacillus subtilis gluconate operon (GntR), the regulators for histidine utilization in Pseudomonas putida (HutCPp) and Klebsiella aerogenes (HutCKa), the repressor (FadR) of fatty acid degradation in Escherichia coli, a regulator involved in the conjugal transfer of the broad host range plasmid pIJ101 (KorA), and three proteins of unidentified function in E. coli (GenA, P30 and PhnF). The proteins share amino acid sequence similarities in a 69-residue N-terminal region. A helix-turn-helix motif is predicted in the most highly-conserved segment of each protein suggesting that they are members of a new family of helix-turn-helix DNA-binding proteins.

Key words
  • Helix-turn-helix motif
  • Transcriptional regulator
  • DNA-binding protein
  • Sequence comparison
  • FadR
  • GenA
  • GntR
  • HutC
  • KorA
  • P30
  • PhnF

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