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Literature summary for 3.4.21.89 extracted from

  • Walsh, S.I.; Craney, A.; Romesberg, F.E.
    Not just an antibiotic target exploring the role of type I signal peptidase in bacterial virulence (2016), Bioorg. Med. Chem., 24, 6370-6378 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Streptococcus pneumoniae
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Streptococcus agalactiae
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Corynebacterium diphtheriae
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Listeria monocytogenes
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Actinomyces sp.
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Enterococcus sp.
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Escherichia coli
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Streptococcus gallolyticus
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Pseudomonas aeruginosa
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Staphylococcus aureus
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Staphylococcus epidermidis
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Bacillus cereus
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Lacticaseibacillus rhamnosus
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Streptococcus pyogenes
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Bacillus anthracis
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Clostridioides difficile
drug development bacterial signal peptidase I (SPase) represents an attractive target in that SPase inhibitors exhibit broad-spectrum antibiotic activity, but even at sub-MIC doses also impair the secretion of essential virulence factors Enterococcus faecalis

Inhibitors

Inhibitors Comment Organism Structure
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Actinomyces sp.
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Bacillus anthracis
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Bacillus cereus
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Clostridioides difficile
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Corynebacterium diphtheriae
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Enterococcus faecalis
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Enterococcus sp.
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Escherichia coli
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Lacticaseibacillus rhamnosus
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Listeria monocytogenes
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Pseudomonas aeruginosa
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum. The presence of Staphylococcus aureus proteins in the media fraction is inversely correlated with the arylomycin dose. Among the SPase secretome are many known virulence factors such as membrane damaging toxins, cell wall attached proteins for immune evasion, proteases that cleave host factors, and coagulases that promote prothrombin activation and may lead to protection from phagocytosis Staphylococcus aureus
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum. The presence of Staphylococcus epidermidis proteins in the media fraction is inversely correlated with the arylomycin dose. Among the SPase secretome are many known virulence factors such as membrane damaging toxins, cell wall attached proteins for immune evasion, proteases that cleave host factors, and coagulases that promote prothrombin activation and may lead to protection from phagocytosis Staphylococcus epidermidis
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Streptococcus agalactiae
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Streptococcus gallolyticus
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Streptococcus pneumoniae
arylomycin while arylomycins have activity against a variety of Gram-positive and Gram-negative bacteria, mutations within SPase that ablate a hydrogen bond limit their spectrum Streptococcus pyogenes
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Actinomyces sp.
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Bacillus anthracis
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Bacillus cereus
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Clostridioides difficile
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Corynebacterium diphtheriae
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Enterococcus faecalis
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Enterococcus sp.
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Escherichia coli
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Lacticaseibacillus rhamnosus
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Listeria monocytogenes
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Pseudomonas aeruginosa
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Staphylococcus aureus
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Staphylococcus epidermidis
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Streptococcus agalactiae
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Streptococcus gallolyticus
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Streptococcus pneumoniae
additional information several classes of inhibitors exist for SPase: krisynomycin and the arylomycin family represent natural product inhibitors, whereas 5S penems peptide substrate mimics and a beta-aminoketone are synthetic inhibitors Streptococcus pyogenes

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasmic membrane
-
Streptococcus pneumoniae
-
-
cytoplasmic membrane
-
Streptococcus agalactiae
-
-
cytoplasmic membrane
-
Corynebacterium diphtheriae
-
-
cytoplasmic membrane
-
Listeria monocytogenes
-
-
cytoplasmic membrane
-
Actinomyces sp.
-
-
cytoplasmic membrane
-
Enterococcus sp.
-
-
cytoplasmic membrane
-
Escherichia coli
-
-
cytoplasmic membrane
-
Streptococcus gallolyticus
-
-
cytoplasmic membrane
-
Pseudomonas aeruginosa
-
-
cytoplasmic membrane
-
Staphylococcus aureus
-
-
cytoplasmic membrane
-
Staphylococcus epidermidis
-
-
cytoplasmic membrane
-
Bacillus cereus
-
-
cytoplasmic membrane
-
Lacticaseibacillus rhamnosus
-
-
cytoplasmic membrane
-
Streptococcus pyogenes
-
-
cytoplasmic membrane
-
Bacillus anthracis
-
-
cytoplasmic membrane
-
Clostridioides difficile
-
-
cytoplasmic membrane
-
Enterococcus faecalis
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Staphylococcus epidermidis autolysin E (AtlE), accumulation-associated protein (AAP), Bap, extracellular matrix protein (Ebh), and the surface protein SSP1, have all been implicated in biofilm formation, and each are predicted to be SPase substrates ?
-
?
additional information Streptococcus pneumoniae the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria ?
-
?
additional information Streptococcus agalactiae the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria ?
-
?
additional information Corynebacterium diphtheriae the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria ?
-
?
additional information Actinomyces sp. the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria ?
-
?
additional information Enterococcus sp. the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria ?
-
?
additional information Streptococcus gallolyticus the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria ?
-
?
additional information Bacillus cereus the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria ?
-
?
additional information Lacticaseibacillus rhamnosus the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria ?
-
?
additional information Streptococcus pyogenes the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria ?
-
?
additional information Staphylococcus epidermidis ATCC 35984 autolysin E (AtlE), accumulation-associated protein (AAP), Bap, extracellular matrix protein (Ebh), and the surface protein SSP1, have all been implicated in biofilm formation, and each are predicted to be SPase substrates ?
-
?
additional information Bacillus cereus 03BB108 the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria ?
-
?

Organism

Organism UniProt Comment Textmining
Actinomyces sp.
-
-
-
Bacillus anthracis A0A1S0QR24
-
-
Bacillus cereus A0A7D3YGV4
-
-
Bacillus cereus 03BB108 A0A7D3YGV4
-
-
Clostridioides difficile A0A031W9H6
-
-
Corynebacterium diphtheriae
-
-
-
Enterococcus faecalis A0A1B4XP47
-
-
Enterococcus sp.
-
-
-
Escherichia coli P00803
-
-
Lacticaseibacillus rhamnosus A0A180C927
-
-
Listeria monocytogenes
-
-
-
Pseudomonas aeruginosa Q9I5G7
-
-
Pseudomonas aeruginosa 1C Q9I5G7
-
-
Pseudomonas aeruginosa ATCC 15692 Q9I5G7
-
-
Pseudomonas aeruginosa CIP 104116 Q9I5G7
-
-
Pseudomonas aeruginosa DSM 22644 Q9I5G7
-
-
Pseudomonas aeruginosa JCM 14847 Q9I5G7
-
-
Pseudomonas aeruginosa LMG 12228 Q9I5G7
-
-
Pseudomonas aeruginosa PRS 101 Q9I5G7
-
-
Staphylococcus aureus P0A070
-
-
Staphylococcus epidermidis Q5HQJ6
-
-
Staphylococcus epidermidis ATCC 35984 Q5HQJ6
-
-
Streptococcus agalactiae
-
-
-
Streptococcus gallolyticus
-
-
-
Streptococcus pneumoniae
-
-
-
Streptococcus pyogenes A0A4U7IU30
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information autolysin E (AtlE), accumulation-associated protein (AAP), Bap, extracellular matrix protein (Ebh), and the surface protein SSP1, have all been implicated in biofilm formation, and each are predicted to be SPase substrates Staphylococcus epidermidis ?
-
?
additional information the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria Streptococcus pneumoniae ?
-
?
additional information the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria Streptococcus agalactiae ?
-
?
additional information the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria Corynebacterium diphtheriae ?
-
?
additional information the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria Actinomyces sp. ?
-
?
additional information the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria Enterococcus sp. ?
-
?
additional information the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria Streptococcus gallolyticus ?
-
?
additional information the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria Bacillus cereus ?
-
?
additional information the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria Lacticaseibacillus rhamnosus ?
-
?
additional information the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria Streptococcus pyogenes ?
-
?
additional information autolysin E (AtlE), accumulation-associated protein (AAP), Bap, extracellular matrix protein (Ebh), and the surface protein SSP1, have all been implicated in biofilm formation, and each are predicted to be SPase substrates Staphylococcus epidermidis ATCC 35984 ?
-
?
additional information the Gram-positive pathogen secretes pilin components that have N-terminal signal peptides with a predicted SPase cleavage site (as well as a C-terminal sortase signal for processing and attachment to the cell wall). Pili in general are important for adherence to host cells, although they serve other functions in specific bacteria Bacillus cereus 03BB108 ?
-
?

Synonyms

Synonyms Comment Organism
LepB
-
Escherichia coli
LepB
-
Listeria monocytogenes
LepB
-
Pseudomonas aeruginosa
LepB
-
Bacillus cereus
LepB
-
Lacticaseibacillus rhamnosus
LepB
-
Streptococcus pyogenes
LepB
-
Bacillus anthracis
LepB
-
Clostridioides difficile
LepB
-
Enterococcus faecalis
Signal peptidase IB
-
Staphylococcus aureus
Signal peptidase IB
-
Staphylococcus epidermidis
SPase
-
Streptococcus pneumoniae
SPase
-
Streptococcus agalactiae
SPase
-
Corynebacterium diphtheriae
SPase
-
Listeria monocytogenes
SPase
-
Actinomyces sp.
SPase
-
Enterococcus sp.
SPase
-
Escherichia coli
SPase
-
Streptococcus gallolyticus
SPase
-
Pseudomonas aeruginosa
SPase
-
Staphylococcus aureus
SPase
-
Staphylococcus epidermidis
SPase
-
Bacillus cereus
SPase
-
Lacticaseibacillus rhamnosus
SPase
-
Streptococcus pyogenes
SPase
-
Bacillus anthracis
SPase
-
Clostridioides difficile
SPase
-
Enterococcus faecalis
SPase IB
-
Staphylococcus aureus
SPase IB
-
Staphylococcus epidermidis
SpsB
-
Staphylococcus aureus
SpsB
-
Staphylococcus epidermidis
type I signal peptidase
-
Streptococcus pneumoniae
type I signal peptidase
-
Streptococcus agalactiae
type I signal peptidase
-
Corynebacterium diphtheriae
type I signal peptidase
-
Listeria monocytogenes
type I signal peptidase
-
Actinomyces sp.
type I signal peptidase
-
Enterococcus sp.
type I signal peptidase
-
Escherichia coli
type I signal peptidase
-
Streptococcus gallolyticus
type I signal peptidase
-
Pseudomonas aeruginosa
type I signal peptidase
-
Staphylococcus aureus
type I signal peptidase
-
Staphylococcus epidermidis
type I signal peptidase
-
Bacillus cereus
type I signal peptidase
-
Lacticaseibacillus rhamnosus
type I signal peptidase
-
Streptococcus pyogenes
type I signal peptidase
-
Bacillus anthracis
type I signal peptidase
-
Clostridioides difficile
type I signal peptidase
-
Enterococcus faecalis

General Information

General Information Comment Organism
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Streptococcus pneumoniae
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Streptococcus agalactiae
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Corynebacterium diphtheriae
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Actinomyces sp.
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Enterococcus sp.
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Escherichia coli
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Streptococcus gallolyticus
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Pseudomonas aeruginosa
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Staphylococcus aureus
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Staphylococcus epidermidis
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Bacillus cereus
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Lacticaseibacillus rhamnosus
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Streptococcus pyogenes
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Bacillus anthracis
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Clostridioides difficile
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death Enterococcus faecalis
malfunction potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death. Deletion of sipZ results in an almost complete loss of infectivity in a mouse model Listeria monocytogenes
metabolism SPase may influence flagellar assembly and type IV secretion systems (T4SSs), as components of the translocation machinery itself are predicted to require SPase processing.79,80 For example, the T4SS mediates the direct transfer of proteins into target cells, but is perhaps best known for its role in the direct transfer of DNA, as this has been implicated as a primary means by which bacteria acquire foreign DNA leading to antibiotic resistance Enterococcus faecalis
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Streptococcus pneumoniae
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Streptococcus agalactiae
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Corynebacterium diphtheriae
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Actinomyces sp.
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Enterococcus sp.
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Escherichia coli
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Streptococcus gallolyticus
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Pseudomonas aeruginosa
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Staphylococcus aureus
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Bacillus cereus
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Lacticaseibacillus rhamnosus
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Streptococcus pyogenes
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Enterococcus faecalis
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. As is common with Gram-positive bacteria, the genome of Listeria monocytogenes includes three separate SPase genes (SipX, SipY, and SipZ) that each play distinct roles in virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Listeria monocytogenes
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. The pathogenicity of Staphylococcus epidermidis relies almost solely on its ability to form biofilms. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Staphylococcus epidermidis
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase is involved in the formation of the S-layer which is a crystalline-like array of proteins, glycoprotein, or both that coat the surface of the cell. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Bacillus anthracis
physiological function type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase is involved in the formation of the S-layer which is a crystalline-like array of proteins, glycoprotein, or both that coat the surface of the cell. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane Clostridioides difficile