3.4.23.36	additional information	indispensability of the cysteine residue for modification and processing, glycine at the -1 position can be replaced by alanine or serine, however, mutant prolipoprotein with leucine or isoleucine substitution at the -1 position are modified and consequently not processed, whereas a glycine to threonine substitution at the -1 position allows modification at a slower rate, but does not allow processing of the lipid-modified mutant prolipoprotein	Escherichia coli	?	-	?	89	
3.4.23.36	additional information	indispensability of the cysteine residue for modification and processing, glycine at the -1 position can be replaced by alanine or serine, however, mutant prolipoprotein with leucine or isoleucine substitution at the -1 position are modified and consequently not processed, whereas a glycine to threonine substitution at the -1 position allows modification at a slower rate, but does not allow processing of the lipid-modified mutant prolipoprotein	Escherichia coli B / ATCC 11303	?	-	?	89	
3.4.23.36	additional information	lipoprotein processing by LspA is required for virulence of the organism and acts as virulence determinant of tuberculosis	Mycobacterium tuberculosis	?	-	?	89	
3.4.23.36	additional information	lipoprotein processing by LspA is required for virulence of the organism and acts as virulence determinant of tuberculosis	Mycobacterium tuberculosis H37Rv	?	-	?	89	
3.4.23.36	additional information	no activity with tumor necrosis factor-alpha, neuregulin 1 type III and Bri2	Mus musculus	?	-	?	89	
3.4.23.36	additional information	not: unmodified precursor of the major lipoprotein	Escherichia coli	?	-	?	89	
3.4.23.36	additional information	processing of prolipoproteins seems to be conserved among different bacterial species, and requires type II signal peptidase mediated cleavage of the N-terminal signal peptide to form the mature lipoprotein. Deletion of Sp0928 prevented processing of Streptococcus pneumoniae prolipoproteins to mature lipoproteins	Streptococcus pneumoniae	?	-	?	89	
3.4.23.36	additional information	processing of the lipid-modified prolipoproteins	Escherichia coli	?	-	?	89	
3.4.23.36	additional information	processing of the lipid-modified prolipoproteins	Escherichia coli B / ATCC 11303	?	-	?	89	
3.4.23.36	additional information	signal peptidases are integral components of the secretory pathway	Escherichia coli	?	-	?	89