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bacterial lipoprotein + H2O
?
Braun's polylipoprotein + H2O
?
Glyceride-containing precursor of new lipoprotein + H2O
?
-
-
-
-
-
Glyceride-containing precursor of the major outer membrane lipoprotein + H2O
?
-
-
-
-
-
Glyceride-containing precursor of the peptidoglycan-associated lipoprotein + H2O
?
-
-
-
-
-
Murein prolipoprotein + H2O
?
pre-PrsA + H2O
PrsA protein + ?
-
-
-
?
additional information
?
-
bacterial lipoprotein + H2O

?
-
cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide
-
-
?
bacterial lipoprotein + H2O
?
-
-
-
-
?
bacterial 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
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide
-
-
?
bacterial 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
-
-
?
bacterial lipoprotein + H2O
?
-
-
-
-
?
bacterial lipoprotein + H2O
?
-
-
-
-
?
bacterial lipoprotein + H2O
?
-
-
-
-
?
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
?
-
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
?
-
-
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
?
-
-
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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bacterial lipoprotein + H2O
?
additional information
?
-
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
?
-
-
-
-
?
bacterial 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
?
-
-
-
-
?
bacterial lipoprotein + H2O
?
-
cleavage of the signal peptide, the enzyme is essential for lipoprotein biosynthesis
-
-
?
bacterial lipoprotein + H2O
?
-
-
-
-
?
bacterial lipoprotein + H2O
?
-
-
-
-
?
bacterial lipoprotein + H2O
?
-
-
-
-
?
additional information

?
-
-
processing of the lipid-modified prolipoproteins
-
-
-
additional information
?
-
-
signal peptidases are integral components of the secretory pathway
-
-
-
additional information
?
-
-
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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A128V
-
site-directed mutagenesis
D102A
-
site-directed mutagenesis
D111A
-
site-directed mutagenesis
D129A
-
site-directed mutagenesis
D14A
-
site-directed mutagenesis
F125A
-
site-directed mutagenesis
F50A
-
site-directed mutagenesis
G47A
-
site-directed mutagenesis
G95A
-
site-directed mutagenesis
K18A
-
site-directed mutagenesis
N126A
-
site-directed mutagenesis
N45A
-
site-directed mutagenesis
N99A
-
site-directed mutagenesis
R103A
-
site-directed mutagenesis
V109A
-
site-directed mutagenesis
W50A
-
site-directed mutagenesis
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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Innis, M.A.; Tokunaga, M.; Williams, M.E.; Loranger, J.M.; Chang, S.Y.; Chang, S.; Wu, H.C.
Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene
Proc. Natl. Acad. Sci. USA
81
3708-3712
1984
Escherichia coli
brenda
Isaki, L.; Kawakami, M.; Beers, R.; Hom, R.; Wu, H.C.
Cloning and nucleotide sequence of the Enterobacter aerogenes signal peptidase II (lsp) gene
J. Bacteriol.
172
469-472
1990
Klebsiella aerogenes
brenda
Yu, F.; Yamada, H.; Daishima, K.; Mizushima, S.
Nucleotide sequence of the lspA gene, the structural gene for lipoprotein signal peptidase of Escherichia coli
FEBS Lett.
173
264-268
1984
Escherichia coli
brenda
Yamada, H.; Yamagata, H.; Mizushima, S.
The major outer membrane lipoprotein and new lipoproteins share a common signal peptidase that exists in the cytoplasmic membrane of Escherichia coli
FEBS Lett.
166
179-182
1984
Escherichia coli
brenda
Dev, I.K.; Ray, P.H.
Signal peptidases and signal peptide hydrolases
J. Bioenerg. Biomembr.
22
271-290
1990
Escherichia coli
brenda
Sankaran, K.; Wu, H.C.
Bacterial prolipoprotein signal peptidase
Methods Enzymol.
248
169-180
1995
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Zhao, X.J.; Wu, H.C.
Nucleotide sequence of the Staphylococcus aureus signal peptidase II (lsp) gene
FEBS Lett.
299
80-84
1992
Staphylococcus aureus
brenda
Tjalsma, H.; Zanen, G.; Venema, G.; Bron, S.; Van Dijl, J.M.
The potential active site of the lipoprotein-specific (type II) signal peptidase of Bacillus subtilis
J. Biol. Chem.
274
28191-28197
1999
Bacillus subtilis
brenda
Sankaran, K.
Signal peptidase II
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
201-204
2004
Bacillus subtilis, Escherichia coli, Klebsiella aerogenes, Myxococcus xanthus, Pseudomonas fluorescens, Staphylococcus aureus
-
brenda
Sander, P.; Rezwan, M.; Walker, B.; Rampini, S.K.; Kroppenstedt, R.M.; Ehlers, S.; Keller, C.; Keeble, J.R.; Hagemeier, M.; Colston, M.J.; Springer, B.; Boettger, E.C.
Lipoprotein processing is required for virulence of Mycobacterium tuberculosis
Mol. Microbiol.
52
1543-1552
2004
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Gonnet, P.; Rudd, K.E.; Lisacek, F.
Fine-tuning the prediction of sequences cleaved by signal peptidase II: a curated set of proven and predicted lipoproteins of Escherichia coli K-12
Proteomics
4
1597-1613
2004
Escherichia coli K-12
brenda
Rahman, M.S.; Ceraul, S.M.; Dreher-Lesnick, S.M.; Beier, M.S.; Azad, A.F.
The lspA gene, encoding the type II signal peptidase of Rickettsia typhi: transcriptional and functional analysis
J. Bacteriol.
189
336-341
2007
Rickettsia typhi
brenda
Khandavilli, S.; Homer, K.A.; Yuste, J.; Basavanna, S.; Mitchell, T.; Brown, J.S.
Maturation of Streptococcus pneumoniae lipoproteins by a type II signal peptidase is required for ABC transporter function and full virulence
Mol. Microbiol.
67
541-557
2008
Streptococcus pneumoniae
brenda
Geukens, N.; De Buck, E.; Meyen, E.; Maes, L.; Vranckx, L.; Van Mellaert, L.; Anne, J.; Lammertyn, E.
The type II signal peptidase of Legionella pneumophila
Res. Microbiol.
157
836-841
2006
Legionella pneumophila
brenda
Arimoto, T.; Igarashi, T.
Role of prolipoprotein diacylglyceryl transferase (Lgt) and lipoprotein-specific signal peptidase II (LspA) in localization and physiological function of lipoprotein MsmE in Streptococcus mutans
Oral Microbiol. Immunol.
23
515-519
2008
Streptococcus mutans (Q8DUQ0), Streptococcus mutans
brenda
Banaei, N.; Kincaid, E.Z.; Lin, S.Y.; Desmond, E.; Jacobs, W.R.; Ernst, J.D.
Lipoprotein processing is essential for resistance of Mycobacterium tuberculosis to malachite green
Antimicrob. Agents Chemother.
53
3799-3802
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Schmaler, M.; Jann, N.J.; Goetz, F.; Landmann, R.
Staphylococcal lipoproteins and their role in bacterial survival in mice
Int. J. Med. Microbiol.
300
155-160
2010
Staphylococcus aureus
brenda
Das, S.; Kanamoto, T.; Ge, X.; Xu, P.; Unoki, T.; Munro, C.L.; Kitten, T.
Contribution of lipoproteins and lipoprotein processing to endocarditis virulence in Streptococcus sanguinis
J. Bacteriol.
191
4166-4179
2009
Streptococcus sanguinis, Streptococcus sanguinis SK36
brenda
Vickerman, M.M.; Flannagan, S.E.; Jesionowski, A.M.; Brossard, K.A.; Clewell, D.B.; Sedgley, C.M.
A genetic determinant in Streptococcus gordonii Challis encodes a peptide with activity similar to that of enterococcal sex pheromone cAM373, which facilitates intergeneric DNA transfer
J. Bacteriol.
192
2535-2545
2010
Streptococcus gordonii
brenda
Xiao, Y.; Gerth, K.; Mueller, R.; Wall, D.
Myxobacteria antibiotic TA (myxovirescin) inhibits type II signal peptidase
Antimicrob. Agents Chemother.
56
2014-2021
2012
Escherichia coli
brenda