The UbiC transcription regulator-associated (UTRA) domain is a conserved ligand-binding domain that has a similar fold to (PUBMED:12757941). It is believed to modulate activity of bacterial transcription factors in response to binding small molecules.
The UbiC transcription regulator-associated (UTRA) domain is a conserved ligand-binding domain that has a similar fold to IPR007440 [ (PUBMED:12757941) ]. It is believed to modulate activity of bacterial transcription factors in response to binding small molecules [ (PUBMED:12757941) ]. Proteins containing this domain include the histidine utilization repressor (expressed from the hutC gene in Pseudomonas putida), which binds to the hutP region in the histidine utilisation (hut) operon and blocks the expression of all the hut genes in the absence of inducer [ (PUBMED:2203754) ].
GO process:
regulation of transcription, DNA-templated (GO:0006355)
HutC/FarR-like bacterial transcription factors of the GntR family containa small molecule-binding domain of the chorismate lyase fold.
FEMS Microbiol Lett. 2003; 222: 17-23
Display abstract
Numerous bacterial transcription factors contain a DNA-bindinghelix-turn-helix domain and a signaling domain, linked together in asingle polypeptide. Typically, this signaling domain is asmall-molecule-binding domain that undergoes a conformational change uponrecognizing a specific ligand. The HutC/FarR-like transcription factors ofthe GntR family are one of the largest groups of transcription factors inthe proteomes of most free-living bacteria. Using sensitive sequenceprofile analysis we show that the HutC/FarR-like transcription factorscontain a conserved ligand-binding domain, which possesses the same foldas chorismate lyase (Escherichia coli UbiC gene product). Thisrelationship suggests that the C-terminal domain of the HutC/FarR-liketranscription factors binds small molecules in a cleft similar to thesubstrate-binding site of the chorismate lyases. The sequence diversitywithin the predicted binding cleft of the HutC/FarR ligand-binding domainsis consistent with the ability of these transcription factors to respondto diverse small molecules, such as histidine (HutC), fatty acids (FarR),sugars (TreR) and alkylphosphonate (PhnF). UbiC-like chorismate lyasesfunction in the ubiquinone biosynthesis pathway, and have characteristiccharged, catalytic residues. Genome comparisons reveal that chorismatelyase orthologs are found in several bacteria, chloroplasts of eukaryoticalgae and euryarchaea. In contrast, the GntR transcription regulators lackthe conserved catalytic residues of the chorismate lyases, and have so farbeen detected only in bacteria. An ancestral, genericsmall-molecule-binding domain appears to have given rise to the enzymaticand non-catalytic ligand-binding versions of the same fold under theinfluence of different selective pressures.
Structural Genomics, the crystal structure of the C-terminal domain of histidine utilization repressor from Pseudomonas syringae pv. tomato str. DC3000
