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bacterial lipoprotein + H2O
?
Braun's polylipoprotein + H2O
?
FKBP8 + H2O
?
-
i.e. SCSLVLEHQPDNIK
-
-
?
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
?
-
-
-
-
?
heme oxygenase 1 + H2O
?
-
-
-
-
?
invariant chain CD74 of the major histocompatibility II complex + H2O
?
-
-
-
-
?
Murein prolipoprotein + H2O
?
phospholamban + 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
?
-
-
-
-
?
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
-
-
?
prolipoprotein + H2O
?
-
-
-
-
?
prolipoprotein + H2O
?
-
-
-
-
?
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
?
-
-
no activity with tumor necrosis factor-alpha, neuregulin 1 type III and Bri2
-
-
?
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
?
FKBP8 + H2O
?
-
i.e. SCSLVLEHQPDNIK
-
-
?
heme oxygenase 1 + H2O
?
-
-
-
-
?
invariant chain CD74 of the major histocompatibility II complex + H2O
?
-
-
-
-
?
phospholamban + H2O
?
-
-
-
-
?
additional information
?
-
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
?
-
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
?
-
-
no activity with tumor necrosis factor-alpha, neuregulin 1 type III and Bri2
-
-
?
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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Alzheimer Disease
Exome-wide age-of-onset analysis reveals exonic variants in ERN1 and SPPL2C associated with Alzheimer's disease.
Arthritis, Psoriatic
Impaired proteolysis by SPPL2a causes CD74 fragment accumulation that can be recognized by anti-CD74 autoantibodies in human ankylosing spondylitis.
Arthritis, Rheumatoid
Impaired proteolysis by SPPL2a causes CD74 fragment accumulation that can be recognized by anti-CD74 autoantibodies in human ankylosing spondylitis.
Autoimmune Diseases
Discovery of the First Potent, Selective, and Orally Bioavailable Signal Peptide Peptidase-Like 2a (SPPL2a) Inhibitor Displaying Pronounced Immunomodulatory Effects In Vivo.
Autoimmune Diseases
Identification of SPPL2a Inhibitors by Multiparametric Analysis of a High-Content Ultra-High-Throughput Screen.
Autoimmune Diseases
The association of clinical phenotypes to known AD/FTD genetic risk loci and their inter-relationship.
Ehrlichiosis
Proteomic analysis of and immune responses to Ehrlichia chaffeensis lipoproteins.
Frontotemporal Lobar Degeneration
Regulated intramembrane proteolysis of the frontotemporal lobar degeneration risk factor, TMEM106B, by signal peptide peptidase-like 2a (SPPL2a).
Glioblastoma
ODZ1 allows glioblastoma to sustain invasiveness through a Myc-dependent transcriptional upregulation of RhoA.
Infections
LspA inactivation in Mycobacterium tuberculosis results in attenuation without affecting phagosome maturation arrest.
Infections
Proteomic analysis of and immune responses to Ehrlichia chaffeensis lipoproteins.
Mastitis
In the absence of Lgt, lipoproteins are shed from Streptococcus uberis independently of Lsp.
Neoplasms
A genome-wide association study of psoriasis and psoriatic arthritis identifies new disease Loci.
Neoplasms
Non-canonical Shedding of TNF? by SPPL2a Is Determined by the Conformational Flexibility of Its Transmembrane Helix.
Neoplasms
SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production.
signal peptidase ii deficiency
B cell survival, surface BCR and BAFFR expression, CD74 metabolism, and CD8- dendritic cells require the intramembrane endopeptidase SPPL2A.
signal peptidase ii deficiency
Deficiency of the Intramembrane Protease SPPL2a Alters Antimycobacterial Cytokine Responses of Dendritic Cells.
signal peptidase ii deficiency
Disruption of an antimycobacterial circuit between dendritic and helper T cells in human SPPL2a deficiency.
signal peptidase ii deficiency
Mendelian susceptibility to mycobacterial disease: 2014-2018 update.
signal peptidase ii deficiency
Mendelian susceptibility to mycobacterial disease: recent discoveries.
signal peptidase ii deficiency
Processing of CD74 by the Intramembrane Protease SPPL2a Is Critical for B Cell Receptor Signaling in Transitional B Cells.
signal peptidase ii deficiency
The intramembrane protease SPPL2c promotes male germ cell development by cleaving phospholamban.
Spondylitis, Ankylosing
Impaired proteolysis by SPPL2a causes CD74 fragment accumulation that can be recognized by anti-CD74 autoantibodies in human ankylosing spondylitis.
Tuberculosis
Lipoprotein processing is essential for resistance of Mycobacterium tuberculosis to malachite green.
Tuberculosis
Lipoproteins are major targets of the polyclonal human T cell response to Mycobacterium tuberculosis.
Tuberculosis
LspA inactivation in Mycobacterium tuberculosis results in attenuation without affecting phagosome maturation arrest.
Tuberculosis
LspA-independent action of globomycin on Mycobacterium tuberculosis.
Tuberculosis
Potent Inhibition of Macrophage Responses to IFN-{gamma} by Live Virulent Mycobacterium tuberculosis Is Independent of Mature Mycobacterial Lipoproteins but Dependent on TLR2.
Tuberculosis
TLR2-Modulating Lipoproteins of the Mycobacterium tuberculosis Complex Enhance the HIV Infectivity of CD4+ T Cells.
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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
Klebsiella aerogenes, Bacillus subtilis, Escherichia coli, Staphylococcus aureus, Myxococcus xanthus, Pseudomonas fluorescens
-
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
Huettl, S.; Helfrich, F.; Mentrup, T.; Held, S.; Fukumori, A.; Steiner, H.; Saftig, P.; Fluhrer, R.; Schroeder, B.
Substrate determinants of signal peptide peptidase-like 2a (SPPL2a)-mediated intramembrane proteolysis of the invariant chain CD74
Biochem. J.
473
1405-1422
2016
Mus musculus
brenda
Niemeyer, J.; Mentrup, T.; Heidasch, R.; Mueller, S.A.; Biswas, U.; Meyer, R.; Papadopoulou, A.A.; Dederer, V.; Haug-Kroeper, M.; Adamski, V.; Luellmann-Rauch, R.; Bergmann, M.; Mayerhofer, A.; Saftig, P.; Wennemuth, G.; Jessberger, R.; Fluhrer, R.; Lichtenthaler, S.F.; Lemberg, M.K.; Schroeder, B.
The intramembrane protease SPPL2c promotes male germ cell development by cleavingphospholamban
EMBO Rep.
20
e46449
2019
Mus musculus
brenda
Hsu, F.F.; Chou, Y.T.; Chiang, M.T.; Li, F.A.; Yeh, C.T.; Lee, W.H.; Chau, L.Y.
Signal peptide peptidase promotes tumor progression via facilitating FKBP8 degradation
Oncogene
38
1688-1701
2019
Homo sapiens
brenda
Vogeley, L.; El Arnaout, T.; Bailey, J.; Stansfeld, P.J.; Boland, C.; Caffrey, M.
Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin
Science
351
876-880
2016
Pseudomonas aeruginosa
brenda
Paetzel, M.
Bacterial signal peptidases
Subcell. Biochem.
92
187-219
2019
Escherichia coli
brenda