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Information on EC 3.4.23.36 - Signal peptidase II
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3.4.23.36 Signal peptidase IISpecify your search results
Word Map
- 3.4.23.36
- globomycin
-
intramembrane
-
3hpalmitate
-
lipobox
-
lipid-modified
- sppl2b
-
diacylglyceryl
-
isoleucyl-trna
-
spp-like
-
triacylated
-
intramembrane-cleaving
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
signal peptidase ii, sppl2a, lipoprotein signal peptidase, prolipoprotein signal peptidase, spase ii, sppl2c, signal peptide peptidase-like 2a, type ii signal peptidase, lipoprotein-specific signal peptidase, lipoprotein signal peptidase ii, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
lipoprotein signal peptidase
lipoprotein signal peptidase II
lipoprotein-specific signal peptidase
LspA
SPase II
type II signal peptidase
additional information
additional information
-
the enzyme belongs to the A8 peptidase family
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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
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PATHWAY SOURCE
PATHWAYS
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CAS REGISTRY NUMBER
COMMENTARY
171715-14-3
-
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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
-
?
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
?
-
-
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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NATURAL SUBSTRATE
NATURAL 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
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
-
-
?
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
?
-
-
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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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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INHIBITOR
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
-
detergent
-
required for activity, e.g. Triton X-100 or Nikkol, but not lauryl sarcoside or octylglucoside
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
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
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
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
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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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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
-
brenda
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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 generated in the lspA gene result in the ablation of Streptococcus gordonii-cAM373 activity in culture supernatants
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
-
enzyme deficiency leads to a partial loss of elongated spermatids and reduced motility of mature spermatozoa, but preserved fertility
malfunction
-
enzyme downregulation suppresses tumor cell colony formation, migration, and invasion in vitro
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
-
a cell wall permeability defect is likely responsible for the hypersensitivity of lspA mutant to malachite green
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
-
the enzyme promotes male germ cell development by cleavingxa0phospholamban
physiological function
-
the enzyme promotes tumor progression via facilitating FKBP8 degradation
physiological function
-
lipoprotein processing by lipoprotein signal peptidase II is essential for resistance of Mycobacterium tuberculosis to malachite green
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Staphylococcus aureus (strain MRSA252)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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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SUBUNIT
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
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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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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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