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peptidase G2 autoproteolytic cleavage domain-containing protein
This domain is found at the very C-terminus of bacteriophage parallel beta-helical tailspike proteins. It carries the enzymic residues that induce autoproteolytic cleavage to bring about maturation of the folding process of the helix in a chaperone-like manner. The domain thus mediates the assembly of a large tailspike protein and then releases itself after maturation. These C-terminal regions that autoproteolytically release themselves after maturation are exchangeable between functionally unrelated N-terminal proteins and have been identified in a number of bacteriophage tailspike proteins [1]. [1]. 21330133. Knitting and snipping: chaperones in beta-helix folding. Schulz EC, Ficner R;. Curr Opin Struct Biol. 2011; [Epub ahead of print] (from Pfam)
Pgu1 and Peptidase_G2 domain-containing protein
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