HTH_DEORhelix_turn_helix, Deoxyribose operon repressor
|SMART accession number:||SM00420|
|Interpro abstract (IPR001034):|
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 the Escherichia coli protein 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 oligomerisation domain. DeoR occurs as an octamer, whilst glpR and agaR are tetramers. Several operators may be bound simultaneously, which could facilitate DNA looping [(PUBMED:1731335), (PUBMED:14731281)].
It is worth noting that the DeoR in this entry is represented by the protein, UniProt P0ACK5, from E. coli. Not the DeoR, UniProt P39140, from Bacillus subtilis. Despite sharing the same name, these two proteins do not share protein sequence similarity [(PUBMED:10714997)].
|GO process:||regulation of transcription, DNA-templated (GO:0006355)|
|GO component:||intracellular (GO:0005622)|
|GO function:||sequence-specific DNA binding transcription factor activity (GO:0003700)|
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