Targeting of Atl to the equatorial surface rings of
S. aureus. Autolysin is exported from the bacterial
cytoplasm (A), and extracellular pro-Atl is targeted to receptor
molecules representing the equatorial surface rings of staphylococci
that mark the future cell division site (B). Targeting requires the
repeats domains (R1 to R3) or pro-Atl. Proteolytic cleavage of pro-Atl
generates mature amidase (Atl-A) and glucosaminidase (Atl-G), each of
which retains one or two repeat domains and remains bound to the
surface rings. The enzymes hydrolyze the cell wall at the cell division
site, an event that is probably synchronized with intracellular
contraction of FtsZ rings (C), thereby generating two fully separated
daughter cells (D). In staphylococci, division occurs perpendicular to
the previous cell division plane and targeting of pro-Atl to the second
equatorial surface ring can initiate hydrolysis at the future cell
division site.