SPase II cleaves signal peptides from prolipoproteins, enabling their anchoring to bacterial membranes. In T. elongatus, lspA shares conserved residues with homologs in Rickettsia typhi and E. coli, confirming its catalytic role .
Globomycin Resistance: Overexpression of T. elongatus lspA in E. coli confers resistance to globomycin (a SPase II inhibitor), validating its activity .
Genetic Complementation: In E. coli strain Y815 (temperature-sensitive SPase II mutant), T. elongatus lspA restored growth at 42°C, albeit with lower efficiency (~4.7%) compared to E. coli lspA (~21.5%) .
Substrate Specificity: Preferentially processes lipoproteins amidated on the d-iso-glutamyl residue, as inferred from structural homology with Rickettsia spp. and E. coli SPase II .
Recombinant T. elongatus lspA offers opportunities in:
KEGG: tel:tlr2420
STRING: 197221.tlr2420