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The C-terminal processing protease, CtpB (YvjB). Crystal structures reflecting distinct functional states show that CtpB constitutes a ring-like protein scaffold penetrated by two narrow tunnels. Access to the proteolytic sites sequestered within these tunnels is controlled by PDZ domains that rearrange upon substrate binding. Accordingly, CtpB resembles a minimal version of a self-compartmentalizing protease regulated by a unique allosteric mechanism (Mastny et al. 2013).  May show limited sequence similarity with 8.A.24.1.1.  The transmembrane domain serves as a receptor for the LsbB bacteriocin in Lactococcus lactis (Miljkovic et al. 2016).

CtpB of Bacillus subtilis

Tail-specific protease, Prc or Tsp, of 682 aas and 1 N-terminal TMS.  Similar to 9.B.174.1.1 only in the central hydrophilic region. Prc, together with an outer membrane lipoprotein, NlpI, contributes to growth and enlargement of the peptidoglycan sacculus by modulating the cellular levels of the cross-link-cleaving hydrolase, MepS. It thus contributes to growth and enlargement of the PG sacculus (Singh et al. 2015).

Prc of E. coli