|PROSITE documentation PDOC00696|
The deoR-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 50-60 amino acids present in transcription regulators of the deoR family, involved in sugar catabolism. This family of prokaryotic regulators is named after Escherichia coli deoR, a repressor of the deo operon, which encodes nucleotide and deoxyribonucleotide catabolic enzymes. DeoR also negatively regulates the expression of nupG and tsx, a nucleoside-specific transport protein and a channel-forming protein, respectively.
DeoR-like transcription repressors occur in diverse bacteria as regulators of sugar and nucleoside metabolic systems. The effector molecules for deoR-like regulators are generally phosphorylated intermediates of the relevant metabolic pathway. The DNA-binding deoR-type HTH domain occurs usually in the N-terminal part. The C-terminal part can contain an effector-binding domain and/or an oligomerization domain. DeoR occurs as an octamer, whilst glpR and agaR are tetramers. Several operators may be bound simultaneously, which could facilitate DNA looping [1,2,3].
Some proteins known to contain a deoR-type HTH domain:
The pattern we use to detect these proteins starts fourteen residues before the HTH motif and ends one residue after it. The profile we developed extends seventeen residues upstream and seventeen residues downstream of the HTH extremities and covers the entire deoR-type HTH DNA-binding domain.Note:
The deoR repressor from Bacillus subtilis, which regulates expression of the dra-nupC-pdp operon required for deoxyribonucleoside and deoxyribose utilization, shows no sequence similarity to E. coli deoR. There is no similarity in the DNA operator sites either and the B. subtilis deoR does not possess a deoR-type HTH domain.Last update:
December 2004 / Pattern and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Beck von Bodman S. Hayman G.T. Farrand S.K.|
|Title||Opine catabolism and conjugal transfer of the nopaline Ti plasmid pTiC58 are coordinately regulated by a single repressor.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 89:643-647(1992).|
|Source||Unpublished observations (1993).|
|3||Authors||Ray W.K. Larson T.J.|
|Title||Application of AgaR repressor and dominant repressor variants for verification of a gene cluster involved in N-acetylgalactosamine metabolism in Escherichia coli K-12.|
|Source||Mol. Microbiol. 51:813-826(2004).|