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Enzyme Nomenclature
Information on EC 3.4.23.36 - Signal peptidase II
for references in articles please use BRENDA:EC3.4.23.36
Word Map on EC 3.4.23.36
- 3.4.23.36
- globomycin
-
3hpalmitate
-
diacylglyceryl
-
lipid-modified
-
lipobox
-
isoleucyl-trna
-
leptospiral
- kirschneri
-
triacylated
-
braun
-
n-acyltransferase
- medicine
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.4.23.36
-
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RECOMMENDED NAME
GeneOntology No.
Signal peptidase II
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Xaa is hydrophobic (preferably Leu) and Xbb (Ala or Ser) and Xcc (Gly or Ala) have small, neutral side chains, release of signal peptides from bacterial membrane prolipoproteins including murein prolipoprotein
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
aspartic endopeptidase
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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CAS REGISTRY NUMBER
COMMENTARY
171715-14-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
a cell wall permeability defect is likely responsible for the hypersensitivity of lspA mutant to malachite green
malfunction
-
mutations in lspA gene reduce competitiveness by 2-3fold in the animal model and in broth culture, the lspA mutant has a general defect in lipoprotein cleavage
malfunction
-
mutations generated in the lspA gene result in the ablation of Streptococcus gordonii-cAM373 activity in culture supernatants
malfunction
-
a cell wall permeability defect is likely responsible for the hypersensitivity of lspA mutant to malachite green
-
malfunction
-
mutations in lspA gene reduce competitiveness by 2-3fold in the animal model and in broth culture, the lspA mutant has a general defect in lipoprotein cleavage
-
physiological function
-
lipoprotein processing by lipoprotein signal peptidase II is essential for resistance of Mycobacterium tuberculosis to malachite green
physiological function
-
overexpression of signal peptides II specifically confers TA resistance to Escherichia coli
physiological function
-
lipoprotein processing by lipoprotein signal peptidase II is essential for resistance of Mycobacterium tuberculosis to malachite green
-
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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
?
-
-
-
-
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
not: unmodified precursor of the major lipoprotein
-
-
-
additional information
?
-
-
processing of the lipid-modified prolipoproteins
-
-
-
additional information
?
-
-
signal peptidases are integral components of the secretory pathway
-
-
-
additional information
?
-
Escherichia coli B / ATCC 11303
-
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
-
-
-
additional information
?
-
Escherichia coli B / ATCC 11303
-
processing of the lipid-modified prolipoproteins
-
-
-
additional information
?
-
-
determination and analysis fo cleavage sequence specificity with diverse lipoprotein substrates, preferred lipoprotein motifs, motif scoring and refinement, detailed overview
-
-
-
additional information
?
-
-
lipoprotein processing by LspA is required for virulence of the organism and acts as virulence determinant of tuberculosis
-
-
-
additional information
?
-
-
lipoprotein processing by LspA is required for virulence of the organism and acts as virulence determinant of tuberculosis
-
-
-
additional information
?
-
-
essential component of lipoprotein processing
-
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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
-
-
?
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
-
-
?
additional information
?
-
-
processing of the lipid-modified prolipoproteins
-
-
-
additional information
?
-
-
signal peptidases are integral components of the secretory pathway
-
-
-
additional information
?
-
Escherichia coli B / ATCC 11303
-
processing of the lipid-modified prolipoproteins
-
-
-
additional information
?
-
-
lipoprotein processing by LspA is required for virulence of the organism and acts as virulence determinant of tuberculosis
-
-
-
additional information
?
-
-
lipoprotein processing by LspA is required for virulence of the organism and acts as virulence determinant of tuberculosis
-
-
-
additional information
?
-
-
essential component of lipoprotein processing
-
-
-
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no requirement for metal ions, thiol reagents, and phospholipids
additional information
-
no requirement for metal ions, thiol reagents, and phospholipids
additional information
-
no requirement for metal ions, thiol reagents, and phospholipids
additional information
-
no requirement for metal ions, thiol reagents, and phospholipids
additional information
-
no requirement for metal ions, thiol reagents, and phospholipids
additional information
-
no requirement for metal ions, thiol reagents, and phospholipids
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Myxobacteria antibiotic TA
-
TA inhibits pro-lipoprotein processing in whole cells, similar to globomycin, thus preventing outer membrane localization of lipoproteins LpoA and LpoB and blocking their essential interactions with PBP1A and PBP1B
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
detergent
-
detergent required for optimal activity in vitro, Triton X-100 and Nikkol support activity; nonionic detergent required for activity
-
detergent
-
detergent required for optimal activity in vitro, Triton X-100 and Nikkol support activity
-
detergent
-
required for activity, e.g. Triton X-100 or Nikkol, but not lauryl sarcoside or octylglucoside
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
transmembrane protein with a large and a small loop at the periplasmic side
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
N-terminal Cys modification with diacylglyceryl before cleavage of the signal peptide to the mature enzyme
additional information
-
N-terminal Cys modification with diacylglyceryl before cleavage of the signal peptide to the mature enzyme
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
in presence of 2% Triton X-100 enzyme can withstand brief exposure up to
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Unstable during purification unless 10% glycerol, 1% Triton X-100, and 1 mM DTT are included in the buffers
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C or -20°C, 10% glycerol, 1% Triton X-100, and 1 mM DTT, stable for at least 1 month
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from inner membrane to homogeneity by solubilization from membrane with Triton X-100, heat treatmemt at 65°C and pH 4.0, anion exchange chromatography, and chromatofocusing, 35000fold, recombinant enzyme by ammonium sulfate fractionation, anion exchange chromatography in presence of EDTA, and gel filtration to homogeneity
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
enzyme overexpression in Escherichia coli confers high resistance to globomycin
-
expression of Sp0928 protects Escherichia coli against the Lsp antagonist globomycin
-
gene lsp, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli under control of the trp promoter
-
ORF Rv1539, gene lspA, from strain H37Rv, DNA and amino acid sequence determination and analysis
-
overexpression of Rickettsia typhi lspA in Escherichia coli confers increased globomycin resistance. Recombinant lspA from significantly restores the growth of temperature-sensitive Escherichia coli Y815 at the nonpermissive temperature, supporting its biological activity as SPase II in prolipoprotein processing
-
wild-type lsp gene amplified by PCR, cloned into pGDL48 and used to transform Bacillus subtilis 8G5lsp, lacking the lsp gene
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
gene lspA disruption mutation by allelic replacement leads to attenuation of virulence and effects viability in murine macrophages, growth and phenotype, overview
additional information
-
gene lspA disruption mutation by allelic replacement leads to attenuation of virulence and effects viability in murine macrophages, growth and phenotype, overview
-
additional information
construction of mutants deficient in diacylglyceryl transferase, lipoprotein-specific signal peptidase II or lipoprotein MsmE. The growth of the diacylglyceryl transferase and lipoprotein-specific signal peptidase II mutants is remarkably reduced in melibiose medium. Lipid modification by diacylglyceryl transferase and subsequent signal peptide cleavage by lipoprotein-specific signal peptidase II are crucial for membrane anchoring and the physiological function of MsmE
additional information
-
construction of mutants deficient in diacylglyceryl transferase, lipoprotein-specific signal peptidase II or lipoprotein MsmE. The growth of the diacylglyceryl transferase and lipoprotein-specific signal peptidase II mutants is remarkably reduced in melibiose medium. Lipid modification by diacylglyceryl transferase and subsequent signal peptide cleavage by lipoprotein-specific signal peptidase II are crucial for membrane anchoring and the physiological function of MsmE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
important role of the enzyme in the pathogenicity of Legionella pneumophila, making it a promising target for therapeutic intervention
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