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Information on EC 3.4.21.89 - Signal peptidase I and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9I5G7
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3.4.21.89 Signal peptidase ISpecify your search results
Word Map
- 3.4.21.89
- polyproteins
- lipoprotein
- preproteins
-
cleavable
- foot-and-mouth
-
unprocessed
-
dyad
-
membrane-spanning
- prolipoproteins
-
translocons
- pilins
-
uncleaved
- beta-lactamase
- drug development
- flavivirus
- ompa
-
nonstructural
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cotranslationally
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co-translational
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sec-dependent
- globomycin
- presequence
-
papain-like
- prepeptide
-
polytopic
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oligonucleotide-directed
- ns2b
-
signal-anchored
- pharmacology
- medicine
- analysis
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
signal peptidase, leader peptidase, spase, protease iv, signal peptidase i, spase i, type i signal peptidase, leader proteinase, plsp1, sec11, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Bacterial leader peptidase 1
-
-
-
-
Escherichia coli leader peptidase
-
-
-
-
Eukaryotic signal peptidase
-
-
-
-
Eukaryotic signal proteinase
-
-
-
-
HOSP
-
-
-
-
Leader peptidase
-
-
-
-
Leader peptidase I
-
-
-
-
Leader peptide hydrolase
-
-
-
-
Leader proteinase
-
-
-
-
Peptidase, signal
-
-
-
-
Pilin leader peptidase
-
-
-
-
Prokaryotic leader peptidase
-
-
-
-
Prokaryotic signal peptidase
-
-
-
-
Prokaryotic signal proteinase
-
-
-
-
Propeptidase
-
-
-
-
Proteinase, eukaryotic signal
-
-
-
-
Proteinase, signal
-
-
-
-
PuIO prepilin peptidase
-
-
-
-
Signal peptidase
-
-
-
-
Signal peptide hydrolase
-
-
-
-
Signal peptide peptidase
-
-
-
-
Signalase
-
-
-
-
SPC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
65979-36-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Dabcyl-VSPAAFAADL(EDANS) + H2O
?
signal peptide of elastase
-
-
?
Dabcyl-VSPAAFAADL(EDANS) + H2O
?
signal peptide of elastase
-
-
?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
tosyl-Gly-Pro-Lys + p-nitroaniline
-
chromozym PL
-
?
Val-Leu-Lys-p-nitroanilide + H2O
Val-Leu-Lys + p-nitroaniline
-
chromozym PL
-
?
additional information
?
-
-
leucine-4-nitroanilide, carbobenzoxy-L-phenylalanyl-L-leucyl-L-alpha-glutamyl-4-nitroanilide, Z-Val-Gly-Arg-4-nitroanilide, benzoyl-beta-alanyl-glycyl-arginine-4-nitroanilide, tosyl-glycyl-prolyl-arginine-4-nitroanilide, and L-Lys-4-nitroanilide are no substrates
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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N-[(1S)-1-(chloroacetyl)-3-methylbutyl]-4-methylbenzenesulfonamide
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total loss of enzyme activity
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
-
additional information
-
not inhibited by thiol-, carboxyl-, or metalloproteinase inhibitors
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
specific activity 471 units/mg, 1 unit is DELTA A/min x total assay volume/sample volume x E 410 nm x light path (cm) where the extinction coefficient E of the product p-nitroanilide at 410 nm is 9.75 and the light path is 0.53 cm
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
-
activity increases from pH 4.0-9.0, 85% of maximal activity at pH 11.0, no activity above pH 12.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
physiological function
the gene is not essential for viability. Similar growth rates are observed for the PA1303 deletion mutant and the wild-type, and in stationary-phase cells no obvious changes in cell morphology are found. Chromosomal deletion mutation leads to the increased secretion of extracellular proteins, increased N-butanoyl homoserine lactone production and influences several quorum-sensing-controlled phenotypic traits, including swarming motility and the production of rhamnolipid and elastinolytic activity
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 80
-
90% of the enzyme activity is abolished by incubation at 60°C for 40 min or 80°C for 1 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
medicine
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developing of medication designed to arrest tissue damage during Pseudomonas infection, opportunistic pathogen causes morbidity and mortality in patients with burns, cystic fibrosis, pneumonia, urinary tract infections, skin infections, cancer, acquired immunodeficiency syndrome, and ocular disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Engel, L.S.; Hill, J.M.; Caballero, A.R.; Green, L.C.; O'Callaghan, R.J.
Protease IV, a unique extracellular protease and virulence factor from Pseudomonas aeruginosa
J. Biol. Chem.
273
16792-16797
1998
Pseudomonas aeruginosa, Pseudomonas aeruginosa PA103-29
Waite, R.D.; Rose, R.S.; Rangarajan, M.; Aduse-Opoku, J.; Hashim, A.; Curtis, M.A.
Pseudomonas aeruginosa possesses two putative type I signal peptidases, LepB and PA1303, each with distinct roles in physiology and virulence
J. Bacteriol.
194
4521-4536
2012
Pseudomonas aeruginosa (Q9I441), Pseudomonas aeruginosa (Q9I5G7), Pseudomonas aeruginosa
Walsh, S.I.; Craney, A.; Romesberg, F.E.
Not just an antibiotic target exploring the role of type I signal peptidase in bacterial virulence
Bioorg. Med. Chem.
24
6370-6378
2016
Actinomyces sp., Corynebacterium diphtheriae, Streptococcus pneumoniae, Listeria monocytogenes, Streptococcus agalactiae, Enterococcus sp., Streptococcus gallolyticus, Clostridioides difficile (A0A031W9H6), Lacticaseibacillus rhamnosus (A0A180C927), Enterococcus faecalis (A0A1B4XP47), Bacillus anthracis (A0A1S0QR24), Streptococcus pyogenes (A0A4U7IU30), Bacillus cereus (A0A7D3YGV4), Escherichia coli (P00803), Staphylococcus aureus (P0A070), Staphylococcus epidermidis (Q5HQJ6), Pseudomonas aeruginosa (Q9I5G7), Pseudomonas aeruginosa ATCC 15692 (Q9I5G7), Pseudomonas aeruginosa 1C (Q9I5G7), Staphylococcus epidermidis ATCC 35984 (Q5HQJ6), Pseudomonas aeruginosa PRS 101 (Q9I5G7), Bacillus cereus 03BB108 (A0A7D3YGV4), Pseudomonas aeruginosa DSM 22644 (Q9I5G7), Pseudomonas aeruginosa CIP 104116 (Q9I5G7), Pseudomonas aeruginosa LMG 12228 (Q9I5G7), Pseudomonas aeruginosa JCM 14847 (Q9I5G7)
EXTERNAL LINKS (specific for EC-Number 3.4.21.89)
Transporter Classification Database (TCDB): 9.B.391.1.3
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