InterPro : IPR000835

Name  MarR-type HTH domain Short Name  HTH_MarR-typ
Type  Domain Description  The MarR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 135 amino acids present in transcription regulators of the MarR/SlyA family, involved in the development of antibiotic resistance. The MarR family of transcription regulators is named after Escherichia coliMarR, a repressor of genes which activate the multiple antibiotic resistance and oxidative stress regulons, and after slyA from Salmonella typhimuriumand E. coli, a transcription regulator that is required for virulence and survival inthe macrophage environment. Regulators with the MarR-type HTH domain arepresent in bacteria and archaea and control a variety of biological functions,including resistance to multiple antibiotics, household disinfectants, organicsolvents, oxidative stress agents and regulation of the virulence factorsynthesis in pathogens of humans and plants. Many of the MarR-like regulatorsrespond to aromatic compounds [, , ].The crystal structures of MarR, MexR and SlyA have been determined and show a winged HTH DNA-binding core flanked by helices involved in dimerisation. The DNA-binding domains are ascribed to the superfamily of wingedhelix proteins, containing a three (four)-helix (H) bundle and a three-stranded antiparallel beta-sheet (B) in the topology: H1-(H1')-H2-B1-H3-H4-B2-B3-H5-H6. Helices 3 and 4 comprise the helix-turn-helix motif and the beta-sheet is called the wing. Helix 4 is termed the recognition helix, like in other HTHs where it binds the DNA major groove. The helices 1, 5 and 6 are involved in dimerisation, as most MarR-like transcription regulators form dimers [, ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

0 Found In

1 Parent Features

Id Name Short Name Type
IPR011991 Winged helix-turn-helix DNA-binding domain WHTH_DNA-bd_dom Domain

4 Publications

First Author Title Year Journal Volume Pages
Alekshun MN The mar regulon: multiple resistance to antibiotics and other toxic chemicals. 1999 Trends Microbiol 7 410-3
Egland PG BadR, a new MarR family member, regulates anaerobic benzoate degradation by Rhodopseudomonas palustris in concert with AadR, an Fnr family member. 1999 J Bacteriol 181 2102-9
Alekshun MN The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution. 2001 Nat Struct Biol 8 710-4
Wu RY Crystal structure of Enterococcus faecalis SlyA-like transcriptional factor. 2003 J Biol Chem 278 20240-4

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)