Disease relevance of yhfN

• The sequence of this putative protease shares high homology with the cell envelope-bound metalloprotease (camelysin) of the closely related species Bacillus cereus [1].
• InhA2 is a homologue of InhA, a Bacillus thuringiensis metalloprotease that specifically degrades antibacterial peptides [2].

High impact information on yhfN

• One enzyme moiety is an adenylate cyclase and the other is a Zn(2+) metalloprotease, which is able to cleave MAPKKs [3].
• The InhA1 metalloprotease allows spores of the B. cereus group to escape macrophages [4].
• We found that these spores survive and escape from macrophages, and that the bacterial metalloprotease InhA1, the major component of the exosporium, is essential for efficient spore release from macrophages [4].
• Although the predicted amino acid sequence of CalY does not exhibit a typical metalloprotease consensus sequence, high-pressure liquid chromatography-purified camelysin contains one zinc ion per protein molecule [5].
• These data together with the amino acid composition, response to metal substitution, chemical modification, and substrate specificity all indicate that this protease is monomeric and is a typical bacterial neutral metalloprotease [6].

References