Signal peptidase SpsB coordinates staphylococcal cell cycle, surface protein septal trafficking, and LTA synthesis.

ABSTRACT: Cell wall-anchored surface proteins of Gram-positive bacteria, harboring a highly conserved YSIRK/G-S signal peptide (SP_YSIRK+), are deposited at cell division septum and anchored to septal peptidoglycan. The mechanisms supporting YSIRK protein septal trafficking remain elusive. Previously, we identified that LtaS-mediated lipoteichoic acid (LTA) synthesis restricts septal trafficking of YSIRK+ proteins in Staphylococcus aureus. Interestingly, both LtaS and SP_YSIRK+ are cleaved by the signal peptidase SpsB, but the biological implications remain unclear. Here, we show that SpsB is required for cleaving SP_SpA(YSIRK+) of staphylococcal surface protein A (SpA). Depletion of spsB not only diminished SP_SpA processing but also abolished S

SUBMITTER: Zhang R 

PROVIDER: S-EPMC11898559 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature