EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.4.23.36 | invariant chain CD74 of the major histocompatibility II complex + H2O |
- |
Mus musculus |
? |
- |
? |
| 3.4.23.36 | more |
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 |
? |
- |
? |
| 3.4.23.36 | more |
not: unmodified precursor of the major lipoprotein |
Escherichia coli |
? |
- |
? |
| 3.4.23.36 | more |
processing of the lipid-modified prolipoproteins |
Escherichia coli |
? |
- |
? |
| 3.4.23.36 | more |
signal peptidases are integral components of the secretory pathway |
Escherichia coli |
? |
- |
? |
| 3.4.23.36 | more |
lipoprotein processing by LspA is required for virulence of the organism and acts as virulence determinant of tuberculosis |
Mycobacterium tuberculosis |
? |
- |
? |
| 3.4.23.36 | more |
active site catalytic residues are Asp102 and Asp129 |
Bacillus subtilis |
? |
- |
? |
| 3.4.23.36 | more |
determination and analysis fo cleavage sequence specificity with diverse lipoprotein substrates, preferred lipoprotein motifs, motif scoring and refinement, detailed overview |
Escherichia coli K-12 |
? |
- |
? |
| 3.4.23.36 | more |
essential component of lipoprotein processing |
Rickettsia typhi |
? |
- |
? |
| 3.4.23.36 | more |
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 |
? |
- |
? |
