Fig. 7
From: Characterization of the major autolysin (AtlC) of Staphylococcus carnosus
Atl is a bifunctional autolysin with different domains post-translationally modified. The complete protein (AtlC) with signal sequence has a length of 136 kDa. When the signal sequence is cleaved, the protein AtlC1 occurs with a length of 133 kDa. In the next step, the propeptide of the two active domains is cut off. AtlC2, with a size of 106 kDa, is formed. Then, the two functional domains (amidase and glucosaminidase) are divided, resulting in fragments AtlC4 and AtlC5 with a size of 50 and 53 kDa. In fragment AtlC3, the two active domains are separated first, leaving the amidase still attached to the propeptide. Fragment Atl3 has a size of 77 kDa. This is the hypothetical cleavage of the AtlC protein and the fragments that can arise and are active and thus can be detected in the zymogram. GW is a cell wall targeting signal and is named after a conserved Gly-Trp (GW) dipeptide