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heme-binding protein
This entry includes haem degrading protein HbpS from Streptomyces reticuli (swiss:Q9RIM2) and and GlcG from Escherichia coli [1]. HbpS is up-regulated in response to haemin- and peroxide-based oxidative stress. It interacts with the SenS/SenR two-component signal transduction system. Iron binds to surface-exposed lysine residues of an octomeric assembly of the protein [2]. The structure of GlcG is composed of an alpha-beta(2)-alpha(3)-beta(2)-alpha fold, similar to the Roadblock/LC7 domain. [1]. 8606183. glc locus of Escherichia coli: characterization of genes encoding the subunits of glycolate oxidase and the glc regulator protein. Pellicer MT, Badia J, Aguilar J, Baldoma L;. J Bacteriol 1996;178:2051-2059. [2]. 19244623. The oligomeric assembly of the novel haem-degrading protein HbpS is essential for interaction with its cognate two-component sensor kinase. Ortiz de Orue Lucana D, Bogel G, Zou P, Groves MR;. J Mol Biol. 2009;386:1108-1122. (from Pfam)
GlcG family protein
GlcG family protein similar to Escherichia coli protein GlcG, part of the glcDEFGB operon, which is induced by growth on glycolate, under the positive control of GlcC
hypothetical protein
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