Open AccessA new family of bacterial regulatory proteins
Author(s) -
Haydon David J.,
Guest John R.
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb04544.x
Subject(s) - pseudomonas putida , operon , helix turn helix , repressor , bacillus subtilis , biology , escherichia coli , peptide sequence , biochemistry , plasmid , conserved sequence , genetics , dna , gene , bacteria , transcription factor
Summary 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 (HutC Pp ) and Klebsiella aerogenes (HutC Ka ), 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.