{PDOC51118} {PS51118; HTH_HXLR} {BEGIN} ******************************** * HxlR-type HTH domain profile * ******************************** The hxlR-type HTH domain is a domain of ~90-100 amino acids present in putative transcription regulators with a winged helix-turn-helix (wHTH) structure. The domain is named after Bacillus subtilis hxlR, a transcription activator of the hxlAB operon involved in the detoxification of formaldehyde [1]. The hxlR-type domain forms the core of putative transcription regulators and of hypothetical proteins occurring in eubacteria as well as in archaea. The sequence and structure of hxlR-type proteins show similarities with the marR-type wHTH (see ) [2]. The crystal structure of ytfH resembles the DNA-binding domains of winged helix proteins (see ), containing a three helix (H) bundle and a three-stranded antiparallel beta-sheet (B) in the topology: H1-H2-B1-H3-H4-B2-B3-H5-H6. This topology corresponds with that of the marR-type DNA-binding domain, wherein helices 3 and 4 comprise the helix-turn-helix motif and the beta-sheet is called the wing. Some proteins known to contain a hxlR-type HTH domain: - Bacillus subtilis hxlR, a transcription activator for enzymes of the ribulose monophosphate pathway, which can be induced by formaldehyde. - Escherichia coli and Salmonella typhimurium ytfH, a hypothetical protein. - Fusobacterium mortiferum malR, a potential regulator of the malBH operon involved in the metabolism of sucrose isomers [3]. The profile we developed covers the entire hxlR-type HTH domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: April 2005 / First entry. [ 1] Yasueda H., Kawahara Y., Sugimoto S. "Bacillus subtilis yckG and yckF encode two key enzymes of the ribulose monophosphate pathway used by methylotrophs, and yckH is required for their expression." J. Bacteriol. 181:7154-7160(1999). PubMed=10572115 [ 2] Huffman J.L., Brennan R.G. "Prokaryotic transcription regulators: more than just the helix-turn-helix motif." Curr. Opin. Struct. Biol. 12:98-106(2002). PubMed=11839496 [ 3] Pikis A., Immel S., Robrish S.A., Thompson J. "Metabolism of sucrose and its five isomers by Fusobacterium mortiferum." Microbiology 148:843-852(2002). PubMed=11882720 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}