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expliquer la libération partielle de la protéase, en effet la souche LMD-9 qui présente cette duplication possède sa protéase PRTS uniquement sous forme ancrée. La comparaison de la séquence primaire de la sortase déduite du gène srtA, chez les souches 4F44, ND03, LMD-9, PB18O, PB302 et CNRZ307, a montré que les sites catalytique (Arg, Cys, His) et actif (Gly, Lys, Ser, Ala, Thr, Ala) sont bien conservés. Six résidus d'acides aminés sont différents pour la sortase de la souche 4F44 par rapport aux autres souches. Parmi ces six résidus, le remplacement du résidu isoleucyl (I 222 ), important pour la bonne orientation du motif d'ancrage LPNTG au niveau du site actif, par le residu valyl (V 222 ) chez la souche 4F44 pourrait entraîner la libération partielle de PrtS. La séquence C-terminale de la protéase PrtS soluble de la souche 4F44 qui contient le domaine LPNTG a été caractérisée : les 2 peptides trypsiques « QVTQLPNTGENDTK » et « QVTQLPNTGENDTKYYLVPGVIIGLGTLLVSIRR » ont été identifiés en spectrométrie de masse MS/MS (ESI-FT-ICR) La présence de ces 2 peptides contenant le motif LPNTG intact indique que la liaison TG (cible de l'activité endopeptidasique de SrtA) n'est pas hydrolysée. La spécificité de coupure de PrtS de la souche 4F44 a été étudiée sur les protéines du lait : l'utilisation du surnageant de culture contenant la protéase PrtS soluble a montré que la caséine ? est préférentiellement hydrolysée par rapport aux autres protéines. Les sites de clivage sur les différentes caséines ont montrés une large spécificité de coupure vis-à-vis de résidus polaires non chargés et de résidus positivement chargés et de résidus hydrophobes encombrants, et Lys en position P1). Globalement 33 peptides à activité biologique sont obtenus avec cette enzyme ; ces peptides sont inhibiteurs de l'ECA, mitogènes, opioïdes, immunomodulants, antibactériens ,
33 bioactive peptides are obtained with this PrtS ; these peptides are antihypertensives, mitogenics, oipoide, immunomodulantors, antimicrobials ,