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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)
heme-binding protein may degrade heme, sequester iron, and may protect from iron-mediated oxidative stress; similar to Streptomyces reticuli heme-degrading protein HbpS
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