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The '''precursor of ASP''' is composed of 624 amino acids. It contains a signal peptide of 24 amino acids, a catalytic domain, similar to that of subtilisin, and a P domain.
The '''precursor of ASP''' is composed of 624 amino acids. It contains a signal peptide of 24 amino acids, a catalytic domain, similar to that of subtilisin, and a P domain.
The '''maturation of ASP''' is achieved by '''ORF2'''. This protein plays the role of an external chaperone and is necessary for the construction of the stable ASP. Indeed, ASP doesn’t contain any propeptide that is involved in the proper folding of the protein. This is a major difference with an other protein, close to ASP : Kex2 ([[1r64]]) <ref>Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria. Kobayashi H et al. Biol. Chem. 290(17):11130-43 (2015)</ref>
The '''maturation of ASP''' is achieved by [http://figshare.com/articles/Close-up_view_of_the_interaction_site_of_ASP_S336A_with_ORF2_/5496337/1 ORF2]. This protein plays the role of an external chaperone and is necessary for the construction of the stable ASP. Indeed, ASP doesn’t contain any propeptide that is involved in the proper folding of the protein. This is a major difference with an other protein, close to ASP : Kex2 ([[1r64]]) <ref>Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria. Kobayashi H et al. Biol. Chem. 290(17):11130-43 (2015)</ref>


The '''ORF2 protein''' is composed of 152 amino-acids coded by the orf2 gene of 456 base pairs. The N-terminal extension and the C-terminal tail of the protein are implicated in the maturation of ASP. In fact, a complex ASP-ORF2 is formed. This association requires a specific organization of ASP in the space. The <scene name='82/829344/The_p-domain/2'>P-domain</scene> of ASP doesn’t bind to ORF2 but the sixth residue from the C-terminus domain of ORF2 interacts with the non-mature ASP. In the complex, the active site of ASP is blocked. This protects the protein from degradation by others.
The '''ORF2 protein''' is composed of 152 amino-acids coded by the orf2 gene of 456 base pairs. The N-terminal extension and the C-terminal tail of the protein are implicated in the maturation of ASP. In fact, a complex ASP-ORF2 is formed. This association requires a specific organization of ASP in the space. The <scene name='82/829344/The_p-domain/2'>P-domain</scene> of ASP doesn’t bind to ORF2 but the sixth residue from the C-terminus domain of ORF2 interacts with the non-mature ASP. In the complex, the active site of ASP is blocked. This protects the protein from degradation by others.