InterPro : IPR020899

Name  Arginine repressor, C-terminal Short Name  Arg_repress_C
Type  Domain Description  The arginine dihydrolase (AD) pathway is found in many prokaryotes and some primitive eukaryotes, an example of the latter being Giardia lamblia(Giardia intestinalis) []. The three-enzyme anaerobic pathway breaks down L-arginine to form 1 mol of ATP, carbon dioxide and ammonia. In simpler bacteria, the first enzyme, arginine deiminase, can account for up to 10%of total cell protein [].Most prokaryotic arginine deiminase pathways are under the control of a repressor gene, termed ArgR []. This is a negative regulator, and will only release the arginine deiminase operon for expression in the presence of arginine []. The crystal structure of apo-ArgR from Bacillus stearothermophilushas been determined to 2.5A by means of X-ray crystallography []. The protein exists as a hexamer of identical subunits, and is shown to have six DNA-binding domains, clustered around a central oligomeric core when bound to arginine. It predominantly interacts with A.T residues in ARG boxes. This hexameric protein binds DNA at its N terminus to repress arginine biosyntheis or activate arginine catabolism. Some species have several ArgR paralogs. In a neighbour-joining tree, some of these paralogous sequences show long branches and differ significantly from the well-conserved C-terminal region. The C-terminal domain of the arginine repressor is responsible for aginine binding and multimerisation [, ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

1 Found In

Id Name Short Name Type
IPR001669 Arginine repressor Arg_repress Family

1 Parent Features

Id Name Short Name Type
IPR024946 Arginine repressor C-terminal-like domain Arg_repress_C-like Domain

6 Publications

First Author Title Year Journal Volume Pages
Brown DM Anaerobic bacterial metabolism in the ancient eukaryote Giardia duodenalis. 1998 Int J Parasitol 28 149-64
Maghnouj A The arcABDC gene cluster, encoding the arginine deiminase pathway of Bacillus licheniformis, and its activation by the arginine repressor argR. 1998 J Bacteriol 180 6468-75
Lu CD Characterization of the arginine repressor from Salmonella typhimurium and its interactions with the carAB operator. 1992 J Mol Biol 225 11-24
Ni J Structure of the arginine repressor from Bacillus stearothermophilus. 1999 Nat Struct Biol 6 427-32
Sunnerhagen M Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA. 1997 Nat Struct Biol 4 819-26
Dennis C CA The structure of AhrC, the arginine repressor/activator protein from Bacillus subtilis. 2002 Acta Crystallogr D Biol Crystallogr 58 421-30

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)