3.4.23.36 bacterial lipoprotein + H2O - Staphylococcus aureus ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O - Escherichia coli ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O - Mycobacterium tuberculosis ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O - Streptococcus sanguinis ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O - Streptococcus gordonii ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Staphylococcus aureus ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Bacillus subtilis ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Escherichia coli ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Pseudomonas fluorescens ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Klebsiella aerogenes ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis Myxococcus xanthus ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Staphylococcus aureus ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Bacillus subtilis ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Escherichia coli ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Pseudomonas fluorescens ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Klebsiella aerogenes ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O cleavage of the signal peptide Myxococcus xanthus ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O - Streptococcus sanguinis SK36 ? - ? 383082 3.4.23.36 bacterial lipoprotein + H2O - Mycobacterium tuberculosis H37Rv ? - ? 383082 3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Staphylococcus aureus ? - ? 384372 3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Bacillus subtilis ? - ? 384372 3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Escherichia coli ? - ? 384372 3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Pseudomonas fluorescens ? - ? 384372 3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Klebsiella aerogenes ? - ? 384372 3.4.23.36 Braun's polylipoprotein + H2O cleavage of the signal peptide, cleavage site specificity, overview Myxococcus xanthus ? - ? 384372 3.4.23.36 FKBP8 + H2O i.e. SCSLVLEHQPDNIK Homo sapiens ? - ? 448588 3.4.23.36 Glyceride-containing precursor of new lipoprotein + H2O - Escherichia coli ? - ? 16508 3.4.23.36 Glyceride-containing precursor of the major outer membrane lipoprotein + H2O - Escherichia coli ? - ? 16507 3.4.23.36 Glyceride-containing precursor of the peptidoglycan-associated lipoprotein + H2O - Escherichia coli ? - ? 16506 3.4.23.36 heme oxygenase 1 + H2O - Mus musculus ? - ? 448668 3.4.23.36 invariant chain CD74 of the major histocompatibility II complex + H2O - Mus musculus ? - ? 448709 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 not: unmodified precursor of the major lipoprotein Escherichia coli ? - ? 89 3.4.23.36 additional information processing of the lipid-modified prolipoproteins Escherichia coli ? - ? 89 3.4.23.36 additional information signal peptidases are integral components of the secretory pathway Escherichia coli ? - ? 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 active site catalytic residues are Asp102 and Asp129 Bacillus subtilis ? - ? 89 3.4.23.36 additional information determination and analysis fo cleavage sequence specificity with diverse lipoprotein substrates, preferred lipoprotein motifs, motif scoring and refinement, detailed overview Escherichia coli K-12 ? - ? 89 3.4.23.36 additional information essential component of lipoprotein processing Rickettsia typhi ? - ? 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 no activity with tumor necrosis factor-alpha, neuregulin 1 type III and Bri2 Mus musculus ? - ? 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 processing of the lipid-modified prolipoproteins 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 H37Rv ? - ? 89 3.4.23.36 Murein prolipoprotein + H2O cleavage of Gly-diacylglyceryl-cysteine bond, also cleavage of this bond in the majority of other lipoprotein precursors, some prolipoproteins contain Ala-diacylglyceryl-cysteine, or Ser-diacylglyceryl-cysteine cleavage sites Escherichia coli ? - ? 16509 3.4.23.36 Murein prolipoprotein + H2O cleavage of Gly-diacylglyceryl-cysteine bond, also cleavage of this bond in the majority of other lipoprotein precursors, some prolipoproteins contain Ala-diacylglyceryl-cysteine, or Ser-diacylglyceryl-cysteine cleavage sites Escherichia coli B / ATCC 11303 ? - ? 16509 3.4.23.36 phospholamban + H2O - Mus musculus ? - ? 448843 3.4.23.36 pre-PrsA + H2O - Bacillus subtilis PrsA protein + ? - ? 366997 3.4.23.36 prolipoprotein + H2O - Escherichia coli ? - ? 453155 3.4.23.36 prolipoprotein + H2O - Escherichia coli B / ATCC 11303 ? - ? 453155