Literature summary 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 .

Application

EC Number	Application	Comment	Organism
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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.
3.4.21.89	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.
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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

EC Number	Inhibitors	Comment	Organism
3.4.21.89	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.
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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.
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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.
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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.
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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

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

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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

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

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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.	?	-	?
3.4.21.89	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.	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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	?	-	?
3.4.21.89	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

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

General Information

EC Number	General Information	Comment	Organism
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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.
3.4.21.89	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.
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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.
3.4.21.89	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.
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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
3.4.21.89	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