3.4.23.36: Signal peptidase II
This is an abbreviated version!
For detailed information about Signal peptidase II, go to the full flat file.
Word Map on EC 3.4.23.36
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3.4.23.36
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globomycin
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intramembrane
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3hpalmitate
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sppl2b
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lipobox
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lipid-modified
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diacylglyceryl
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spp-like
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isoleucyl-trna
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braun
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intramembrane-cleaving
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triacylated
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medicine
- 3.4.23.36
- globomycin
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intramembrane
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3hpalmitate
- sppl2b
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lipobox
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lipid-modified
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diacylglyceryl
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spp-like
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isoleucyl-trna
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braun
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intramembrane-cleaving
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triacylated
- medicine
Reaction
Release of signal peptides from bacterial membrane prolipoproteins including murein prolipoprotein. Hydrolyses -Xaa-Yaa-Zaa-/-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral sidechains =
Synonyms
EC 3.4.99.35, Leader peptidase II, lipoprotein signal peptidase, lipoprotein signal peptidase II, lipoprotein-specific (typeII) signal peptidase, lipoprotein-specific signal peptidase, lipoprotein-specific type II signal peptidase, LspA, More, Premurein leader peptidase, Premurein leader proteinase, Premurein-leader peptidase, Prolipoprotein signal peptidase, Proteinase, premurein leader, Signal peptide peptidase, signal peptide peptidase-like 2a, Sp0928, SPase II, SpiI, SPP, SPPL2a, SPPL2c, type II signal peptidase
ECTree
3.4.23.36 Signal peptidase IIAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.36 - Signal peptidase II
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Glyceride-containing precursor of the major outer membrane lipoprotein + H2O
?
-
-
-
-
?
Glyceride-containing precursor of the peptidoglycan-associated lipoprotein + H2O
?
-
-
-
-
?
invariant chain CD74 of the major histocompatibility II complex + H2O
?
-
-
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis
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-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis
-
-
?
Braun's polylipoprotein + H2O
?
-
cleavage of the signal peptide, cleavage site specificity, overview
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-
?
Braun's polylipoprotein + H2O
?
-
cleavage of the signal peptide, cleavage site specificity, overview
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-
?
Braun's polylipoprotein + H2O
?
-
cleavage of the signal peptide, cleavage site specificity, overview
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-
?
Braun's polylipoprotein + H2O
?
-
cleavage of the signal peptide, cleavage site specificity, overview
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-
?
Braun's polylipoprotein + H2O
?
-
cleavage of the signal peptide, cleavage site specificity, overview
-
-
?
Braun's polylipoprotein + H2O
?
-
cleavage of the signal peptide, cleavage site specificity, overview
-
-
?
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
-
-
?
Murein prolipoprotein + H2O
?
Escherichia coli B / ATCC 11303
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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
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-
?
additional information
?
-
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active site catalytic residues are Asp102 and Asp129
-
-
?
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
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-
?
additional information
?
-
-
not: unmodified precursor of the major lipoprotein
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-
?
additional information
?
-
-
processing of the lipid-modified prolipoproteins
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-
?
additional information
?
-
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signal peptidases are integral components of the secretory pathway
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-
?
additional information
?
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Escherichia coli B / ATCC 11303
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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
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-
?
additional information
?
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Escherichia coli B / ATCC 11303
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processing of the lipid-modified prolipoproteins
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-
?
additional information
?
-
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determination and analysis fo cleavage sequence specificity with diverse lipoprotein substrates, preferred lipoprotein motifs, motif scoring and refinement, detailed overview
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-
?
additional information
?
-
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no activity with tumor necrosis factor-alpha, neuregulin 1 type III and Bri2
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-
?
additional information
?
-
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lipoprotein processing by LspA is required for virulence of the organism and acts as virulence determinant of tuberculosis
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-
?
additional information
?
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lipoprotein processing by LspA is required for virulence of the organism and acts as virulence determinant of tuberculosis
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-
?
additional information
?
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essential component of lipoprotein processing
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-
?
additional information
?
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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
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-
?
