Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(4-(4-dimethylaminophenylazo)benzoyl)-AGHDAHASET-(5-((2-aminoethyl)amino)-naphthalene-1-sulfonic acid) + H2O
(4-(4-dimethylaminophenylazo)benzoyl)-AGHDAHA + SET-(5-((2-aminoethyl)amino)-naphthalene-1-sulfonic acid)
(NO2)YFSASALA-KI-(2-aminobenzoyl)K-NH2 + H2O
(NO2)YFSASALA + KI-(2-aminobenzoyl)K-NH2
-
-
-
?
Ac-AGLIARAVTSGA-NH2 + H2O
Ac-AGLIAR + AVTSGA-NH2
-
-
-
?
Ac-AGPRPTRIAFGA-NH2 + H2O
N-acetyl-L-alanine + GPRPTRIAFGA-NH2
-
-
-
?
Ac-AGPTARAVTSGA-NH2 + H2O
Ac-AGPTARA + VTSGA-NH2
-
-
-
?
Ac-AGSASALAKIGA-NH2 + H2O
Ac-AGSASALA + KIGA-NH2
-
-
-
?
Ac-AGVPPLFAMLGA-NH2 + H2O
Ac-AGVPPLF + AMLGA-NH2
-
-
-
?
Acetyl-Trp-Leu-Val-Pro-norleucine-Leu-Ser-Phe-Ala-Ala-Glu-Gly-Asp-Asp-Pro-Ala-NH2 + H2O
Acetyl-Trp-Leu-Val-Pro-norleucine-Leu-Ser-Phe-Ala + Ala-Glu-Gly-Asp-Asp-Pro-Ala-NH2
-
-
-
?
Acetyl-Trp-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile + H2O
?
-
-
-
-
?
Acetyl-Trp-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Ala-Ala-Phe-4-methylcoumaryl-7-amide + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
alkaline phosphatase signal peptide
?
-
clear evidence of a weak peptide-enzyme complex formation. The peptide adopts a U-turn shape originating from the proline residues within the primary sequence that is stabilized by its interaction with the peptidase and leaves key residues of the cleavage region exposed for proteolysis. In dodecylphosphocholine micelles the signal peptide also adopts a U-turn shape comparable with that observed in association with the enzyme. In both environments this conformation is stabilized by the signal peptide phenylalanine side chain-interaction with enzyme or lipid mimetic. In the presence of dodecylphosphocholine, the N-terminal core region residues of the peptide adopt a helical motif and are buried within the membrane. This is consistent with proteolysis of the preprotein occurring while the signal peptide remains in the bilayer and the enzyme active site functions at the membrane surface
-
-
?
alkaline phosphatase signal peptide fused to full-length mammalian cytochrome b5
cytochrome b5
-
amphipatic, chimeric cytochrome b5 precursor
-
?
beta-lactam response sensor BlaR1 + H2O
?
-
presence of extracellular domains of beta-lactam response sensor BlaR1 in the medium is dependent on SPase activity, suggesting that it is cleaved at noncanonical sites within the protein
-
-
?
Clostridium thermocellum cellulose-binding domain containing a signal peptide + H2O
signal peptide + Clostridium thermocellum cellulose-binding domain
-
signal peptidase Sec11a and Sec11b cleave differentially
-
-
?
complement component C1q + H2O
?
-
partially degraded
-
?
core protein of classical swine fever virus + H2O
?
Cytochrome c2 of Rhodobacter sphaeroides + H2O
?
-
-
-
-
?
Dabcyl-AGHDAHASET(EDANS) + H2O
?
-
a substrate constructed based on the C-terminal region of the Staphylococcus epidermidis pre-SceD protein and containing the native SPase I cleavage site
-
-
?
Dabcyl-VSPAAFAADL(EDANS) + H2O
?
signal peptide of elastase
-
-
?
decanoyl-LTPTAKAASKIDD-OH + H2O
decanoyl-LTPTAKA + ASKIDD
envelope protein Toc75 precursor + H2O
mature envelope protein Toc75 + signal peptide
-
-
-
?
Eukaryotic initiation factor eIF-4gamma from rabbit reticulocytes + H2O
?
-
cleavage site Gly479-Arg480
-
-
?
FSASALAKI + H2O
FSASALA + Lys-Ile
hepatitis C virus core protein + H2O
?
hexanoyl-LTPTQAKAASKIDD-OH + H2O
hexanoyl-LTPTQAKA + ASKIDD
-
-
-
?
Hybrid protein pro-OmpA-nuclease A + H2O
?
-
-
-
-
?
IgG + H2O
?
-
partially degraded
-
?
intermediate of cytochrome c peroxidase + H2O
mature cytochrome c peroxidase + peptide
KLTFGTVKPVQAIAGYEWL + H2O
?
-
synthetic peptide substrate, based upon the signal peptide of prestreptokinase from Streptococcus pyogene
-
?
lipoteichoic acid synthase + H2O
?
M13 phage procoat protein + H2O
Free signal peptide + coat protein
mammalian cytochrome b(5) precursor + H2O
?
the processing can occur after almost complete exocytoplasmic translocation of the preprotein is accomplished
-
-
?
Methanococcus voltae S-layer protein + H2O
?
mitochondrial inter membrane space protein IMS
?
-
mitochondrial inner membrane peptidase, complex specificity requirement, cleaves initially synthesized with a bipartite signal sequence that contains a matrix-targeting signal and an IMS sorting signal, specificity of Imp1p and Imp2p is not identical, precursors of the cytochrome oxidase subunit II pre-COXII and cytochrome b2 are processed exclusively by Imp1p, in contrast, the precursor form of cytochrome c1 is exclusively processed by Imp2p
-
?
O-acetyltransferase + H2O
?
octanoyl-LTPTQAKAASKIDD-OH + H2O
octanoyl-LTPTQAKA + ASKIDD
-
-
-
?
p23 + H2O
p21 + ?
-
-
-
-
?
Parathyroid hormone + H2O
?
-
-
-
?
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile + H2O
?
-
-
-
-
?
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile + H2O
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile + ?
-
-
-
-
?
Phe-Ser-Ala-Ser-Ala-Leu-Ala-Lys-Ile-NH2 + H2O
Phe-Ser-Ala-Ser-Ala-Leu-Ala + Lys-Ile-NH2
-
-
-
-
?
plasminogen + H2O
?
-
-
-
?
Pre-beta-lactamase + H2O
beta-Lactamase + ?
Pre-lambda phage receptor + H2O
Lambda Phage receptor + ?
-
-
-
-
?
pre-maltose binding protein + H2O
maltose binding protein + signal peptide
the maltose binding protein (MBP) is mutated to introduce aromatic amino acids (tryptophan, tyrosine and phenylalanine) at P2' of the signal peptidase I cleavage sequence. All mutants with aromatic amino acids at P2' are exported less efficiently as indicated by a slight increase in precursor protein in vivo. Binding of LepB to peptides that encompass the MBP cleavage site are analysed using surface plasmon resonance. The presence of phenylalanine and tyrosine at P2', but not tryptophan, increase to a small extent the amount of preMBP in the sample
-
-
?
pre-SceD protein + H2O
SceD + presequence of pre-SceD
-
substrate of Sip2 and Sip3
-
-
?
Precursor of pea cytochrome f + H2O
Pea cytochrome f + ?
-
-
-
-
?
Precursor of the 23kd photosystem II protein + H2O
23kd Photosystem II protein + ?
-
-
-
-
?
Precursor of the leucine-binding protein + H2O
Leucine-binding protein + ?
Precursors of the exported proteins Skp of E. coli + H2O
Exported proteins Skp of E. coli + ?
-
processed at the authentic site
-
-
?
Premaltose-binding protein + H2O
Maltose-binding protein + ?
preprotein substrate PONA + H2O
protein substrate PONA + ?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
pro-OmpA-nuclease A + H2O
OmpA-nuclease A + ?
-
-
-
-
?
pro-rem + H2O
signal peptide + rem
-
Rev-like export protein encoded by mouse mammary tumor virus. Mutations at both glycosylation positions eliminate detectable rem glycosylation without effect on SP cleavage. Rem protein expression constructs with mutations at position -1, relative to the predicted cleavage site, i.e. G98R or both positions -1 and -3, V96R/G98R are not cleaved by SP-I
-
-
?
propolylipoprotein signal peptide + H2O
?
-
-
-
?
PsbO precursor protein + H2O
mature PcpO + signal peptide
Zea mays oxygen-evolving enhancer protein 3-1, chloroplastic. Activity is reduced below 10% in Pbs mutant A83L
-
-
?
signal peptidase I + H2O
SPase37-204
-
self-cleavage, results in a truncated product
-
?
signal peptides from preproteins + H2O
mature proteins
SpsB + H2O
?
-
self-cleavage
-
-
?
Staphylococcus epidermidis SceD preprotein + H2O
Staphylococcus epidermidis SceD protein + SceD protein prepeptide fragment
-
specific cleavage at a single cleavage site located at the A-S bond
-
-
?
streptokinase precursor + H2O
streptokinase
synaptobrevin + H2O
?
-
tail-anchored integral membrane protein
-
?
Thylakoid lumen protein precursors + H2O
Thylakoid lumen protein + ?
-
-
-
-
?
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
VsiSP-mTNFalpha + H2O
?
-
-
-
?
Y-NO2-FSASALAKIK-2-aminobenzoyl-NH2 + H2O
Y-NO2-FSASALA + KIK-2-aminobenzoyl-NH2
-
-
-
-
?
YFSASALA-4-methylcoumarin-7-amide + H2O
YFSASALA + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
(4-(4-dimethylaminophenylazo)benzoyl)-AGHDAHASET-(5-((2-aminoethyl)amino)-naphthalene-1-sulfonic acid) + H2O
(4-(4-dimethylaminophenylazo)benzoyl)-AGHDAHA + SET-(5-((2-aminoethyl)amino)-naphthalene-1-sulfonic acid)
-
-
-
?
(4-(4-dimethylaminophenylazo)benzoyl)-AGHDAHASET-(5-((2-aminoethyl)amino)-naphthalene-1-sulfonic acid) + H2O
(4-(4-dimethylaminophenylazo)benzoyl)-AGHDAHA + SET-(5-((2-aminoethyl)amino)-naphthalene-1-sulfonic acid)
-
-
-
?
core protein of classical swine fever virus + H2O
?
-
the processing of core protein of classical swine fever virus is conducted by signal peptide peptidase. Inhibition of this enzyme results in a reduced virus yield
-
-
?
core protein of classical swine fever virus + H2O
?
-
C-terminal processing
-
-
?
decanoyl-LTPTAKAASKIDD-OH + H2O
decanoyl-LTPTAKA + ASKIDD
-
-
-
?
decanoyl-LTPTAKAASKIDD-OH + H2O
decanoyl-LTPTAKA + ASKIDD
-
-
-
?
Fibrinogen + H2O
?
-
-
-
?
Fibrinogen + H2O
?
-
-
-
?
FSASALAKI + H2O
FSASALA + Lys-Ile
-
-
-
-
?
FSASALAKI + H2O
FSASALA + Lys-Ile
-
most rapidly cleaved peptide
-
?
hepatitis C virus core protein + H2O
?
-
-
-
-
?
hepatitis C virus core protein + H2O
?
-
signal peptide peptidase-catalyzed cleavage of hepatitis C virus core protein is dispensable for virus budding, but destabilizes the viral capsid
-
-
?
Immunoglobulin + H2O
?
-
-
-
?
Immunoglobulin + H2O
?
-
-
-
?
intermediate of cytochrome c peroxidase + H2O
mature cytochrome c peroxidase + peptide
-
-
-
-
?
intermediate of cytochrome c peroxidase + H2O
mature cytochrome c peroxidase + peptide
-
Pcp1 is involved in processing of the intermediate of cytochrome c peroxidase
-
-
?
lipoteichoic acid synthase + H2O
?
-
-
soluble C-terminal domain has a noncanonical, internal cleavage site
-
?
lipoteichoic acid synthase + H2O
?
-
-
soluble C-terminal domain has a noncanonical, internal cleavage site
-
?
lipoteichoic acid synthase + H2O
?
-
presence of extracellular domains of lipoteichoic acid synthase in the medium is dependent on SPase activity, suggesting that it is cleaved at noncanonical sites within the protein
-
-
?
M13 phage procoat protein + H2O
Free signal peptide + coat protein
-
hydrolysis of a single-Ala-+-Ala- bond, the term-+- depicts the point of cleavage
-
-
?
M13 phage procoat protein + H2O
Free signal peptide + coat protein
-
hydrolysis of a single-Ala-+-Ala- bond, the term-+- depicts the point of cleavage
-
-
?
Methanococcus voltae S-layer protein + H2O
?
-
truncated, his-tagged form
-
?
Methanococcus voltae S-layer protein + H2O
?
-
truncated, his-tagged form
-
?
O-acetyltransferase + H2O
?
-
-
soluble C-terminal domain has a noncanonical, internal cleavage site
-
?
O-acetyltransferase + H2O
?
-
-
soluble C-terminal domain has a noncanonical, internal cleavage site
-
?
plasmin + H2O
?
-
partially degraded
-
?
plasmin + H2O
?
-
partially degraded
-
?
Pre-beta-lactamase + H2O
beta-Lactamase + ?
-
-
-
-
?
Pre-beta-lactamase + H2O
beta-Lactamase + ?
-
-
-
-
?
Precursor of the leucine-binding protein + H2O
Leucine-binding protein + ?
-
-
-
-
?
Precursor of the leucine-binding protein + H2O
Leucine-binding protein + ?
-
-
-
-
?
Premaltose-binding protein + H2O
Maltose-binding protein + ?
-
-
-
-
?
Premaltose-binding protein + H2O
Maltose-binding protein + ?
-
-
-
-
?
preprotein substrate PONA + H2O
protein substrate PONA + ?
-
-
?
preprotein substrate PONA + H2O
protein substrate PONA + ?
-
-
?
Pro-OmpA + H2O
OmpA + ?
-
-
-
-
?
Pro-OmpA + H2O
OmpA + ?
-
of E. coli
-
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
-
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
-
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
-
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
-
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
-
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
-
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
hybrid secretory precursor, best substrate in vitro, fusion protein consisting of the signal peptide of the E. coli outer membrane protein A OmpA attached to the Staphylococcus aureus nuclease A protein
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
hybrid secretory precursor, best substrate in vitro, fusion protein consisting of the signal peptide of the Escherichia coli outer membrane protein A OmpA attached to the Staphylococcus aureus nuclease A protein
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
excellent substrate for microsomal signal peptidase
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
-
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
cleaves the precursors of many membrane and secreted proteins to their mature products, including most bacterial pre-proteins, yeast pre-acid phosphatase, honeybee pre-pro-mellitin, and human pre-hormones such as pre-pro-insulin, pre-growth hormone, preinterferon and others, can cleave several thylakoidal precursor proteins
-
?
signal peptides from preproteins + H2O
mature proteins
-
in vivo, type I signal peptidase is the principal peptidase responsible for signal peptide cleavage as pre-proteins of a number of exported proteins, proteins designed for transport across the cytoplasmic membrane are generally synthesised as precursors with cleavable signal peptides in the cytoplasm, the signal peptides targets the pre-proteins to the respective translocase, during or shortly after translocation across the cytoplasmic membrane, the signal peptide is enzymatically removed
-
?
signal peptides from preproteins + H2O
mature proteins
-
in vivo, type I signal peptidase is the principal peptidase responsible for signal peptide cleavage as pre-proteins of a number of exported proteins, proteins designed for transport across the cytoplasmic membrane are generally synthesised as precursors with cleavable signal peptides in the cytoplasm, the signal peptides targets the pre-proteins to the respective translocase, during or shortly after translocation across the cytoplasmic membrane, the signal peptide is enzymatically removed
-
?
signal peptides from preproteins + H2O
mature proteins
-
in vivo, type I signal peptidase is the principal peptidase responsible for signal peptide cleavage as pre-proteins of a number of exported proteins, proteins designed for transport across the cytoplasmic membrane are generally synthesised as precursors with cleavable signal peptides in the cytoplasm, the signal peptides targets the pre-proteins to the respective translocase, during or shortly after translocation across the cytoplasmic membrane, the signal peptide is enzymatically removed
-
?
signal peptides from preproteins + H2O
mature proteins
-
key role in the protein secretary pathway
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
streptokinase precursor + H2O
streptokinase
-
extracellular protein, produced in pathogenic streptococci
-
?
streptokinase precursor + H2O
streptokinase
-
extracellular protein, produced in pathogenic streptococci prestreptokinase is the native substrate
-
?
streptokinase precursor + H2O
streptokinase
-
prestreptokinase is the native substrate, to be cleaved between Ala26 and Ile27
-
?
Val-Leu-Lys-p-nitroanilide + H2O
Val-Leu-Lys + p-nitroaniline
-
chromozym PL
-
?
Val-Leu-Lys-p-nitroanilide + H2O
Val-Leu-Lys + p-nitroaniline
-
chromozym PL
-
?
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
-
-
?
additional information
?
-
-
the enzyme is responsible for the full maturation of Toc75, the protein translocation channel at the plastid outer envelope membrane. the enzyme is required for biogenesis of plastid internal membranes
-
-
?
additional information
?
-
-
multiple type I signal peptidase isoforms
-
?
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
-
-
?
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
-
-
?
additional information
?
-
signal peptidase I processes secretory signal sequences. Selection for and against specific amino acids occurs at the second position of mature protein. The enzyme shows preference for the presence of acidic residues at second position of the mature protein (P2'), and a complete absence of aromatic amino acids at the same position. Substrate specificity and in silico prediction of signal peptidase I cleavage sites, overview
-
-
?
additional information
?
-
signal peptidase I processes secretory signal sequences. Selection for and against specific amino acids occurs at the second position of mature protein. The enzyme shows preference for the presence of acidic residues at second position of the mature protein (P2'), and a complete absence of aromatic amino acids at the same position. Substrate specificity and in silico prediction of signal peptidase I cleavage sites, overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
a typical signal sequence is 15-25 amino acids long, it has a tripartite structure consisting of a positively charged NH2-terminal region (n-region, 1-5 amino acids), a central hydrophobic core (h-region, 7-15 amino acids) probably arranged in a alpha-helix, and, separated by an alpha-helix breaking Pro or Gly, the more polar part (c-region, 3-7 amino acids), representing half of the cleavage site
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
cleavage of E. coli enzyme requires a small residue at-1 and a small or aliphatic residue at-3, presence of a helix breaker allows the pre-protein to bind with higher affinity, signal peptides that include a Pro residue at position-1 are not cleaved in E. coli
-
-
?
additional information
?
-
-
minimum sequence of a substrate hydrolyzed is the pentapeptide Ala-Leu-Ala-+-Lys-Ile, the term-+- depicts the point of cleavage
-
-
?
additional information
?
-
-
cleavable pre-proteins must have small residues at-1 and a small or aliphatic residue at-3 (with respect to the cleavage site)
-
-
?
additional information
?
-
-
family of serine proteases that lacks a complete catalytic triad
-
-
?
additional information
?
-
-
a typical signal sequence is 15-25 amino acids long, it has a tripartite structure consisting of a positively charged NH2-terminal region (n-region, 1-5 amino acids), a central hydrophobic core (h-region, 7-15 amino acids) probably arranged in a alpha-helix, and, separated by an alpha-helix breaking Pro or Gly, the more polar part (c-region, 3-7 amino acids), representing half of the cleavage site
-
-
?
additional information
?
-
-
specificity of the thylakoid processing peptidase and E. coli leader peptidase are identical
-
-
?
additional information
?
-
-
requirements for substrate recognition by bacterial leader peptidase
-
-
?
additional information
?
-
-
although the enzyme is unable to cleave an X-Pro bond, a proline at-1 does not prevent the enzyme from recognizing the normal processing site
-
-
?
additional information
?
-
-
specificity: leader peptidase 1 cleaves the majority of the preproteins destined to the cell surface
-
-
?
additional information
?
-
-
the better peptide substrates are those that are able to adopt folded structures
-
-
?
additional information
?
-
-
secretory proteins are synthesized with an aminoterminal extension, the signal peptide, signal peptidases are required for the removal of these extensions
-
?
additional information
?
-
-
the physiological role is to release exported proteins from the membrane by removing the leader sequence
-
-
?
additional information
?
-
-
the enzyme removes amino-terminal leader peptides from exported proteins after they have crossed the plasma membrane
-
-
?
additional information
?
-
-
in addition to naturally occuring precursor protein substrates, signal peptidase can process short, synthetic peptide substrates based on the cleavage site region of pre-maltose binding protein and M13 procoat, minimum length for cleavage of peptide substrates is 5 residues, -3 to + 2 of the pre-maltose binding protein, indicating that the recognition sequence for signal peptidase lies between the -3 and +2 position
-
?
additional information
?
-
-
cleaves the signal peptide of the GST-SP-AP-His construct into two fragments, the GST protein plus the signal peptide (28 kDa), and the first 30 amino acids of the mature region 6-His-tagged (4 kDa)
-
-
?
additional information
?
-
-
substrate binding to SPase I proceeds consistent with induced-fit recognition. Residues Gln85, Ile86, Ser88, Gly89, Ser90, Met91, Leu95, Val132, Asp142, Ile144, and Lys145 in addition to Ile80, Glu82, Ile101, Gly109, and Lys134, are responsive to signal peptide binding and alter conformation
-
-
?
additional information
?
-
SPase I is an essential membrane-bound endopeptidase with a unique Ser/Lys dyad mechanism
-
-
?
additional information
?
-
-
SPase I is an essential membrane-bound endopeptidase with a unique Ser/Lys dyad mechanism
-
-
?
additional information
?
-
-
binding of the signal petide to the sinal peptidase leads to weak peptide-enzyme complex formation. The peptide adopts a U-turn shape originating from the proline residues within the primary sequence that is stabilized by its interaction with the peptidase and leaves key residues of the cleavage region exposed for proteolysis. In dodecylphosphocholine micelles the signal peptide also adopts a U-turn shape comparable with that observed in association with the enzyme. In both environments this conformation is stabilized by the signal peptide phenylalanine side chain-interaction with enzyme or lipid mimetic. In the presence of dodecylphosphocholine, the N-terminal core region residues of the peptide adopt a helical motif are buried within the membrane
-
-
?
additional information
?
-
cleavage site specificity of Escherichia coli SPase I, overview. Cobstruction of different signal peptides of MBP and binding analysis with the enzyme
-
-
?
additional information
?
-
-
cleavage site specificity of Escherichia coli SPase I, overview. Cobstruction of different signal peptides of MBP and binding analysis with the enzyme
-
-
?
additional information
?
-
signal peptidase I processes secretory signal sequences. Selection for and against specific amino acids occurs at the second position of mature protein. The enzyme shows preference for the presence of acidic residues at second position of the mature protein (P2'), and a complete absence of aromatic amino acids at the same position. Substrate specificity and in silico prediction of signal peptidase I cleavage sites, overview
-
-
?
additional information
?
-
-
specificity: leader peptidase 1 cleaves the majority of the preproteins destined to the cell surface
-
-
?
additional information
?
-
-
the physiological role is to release exported proteins from the membrane by removing the leader sequence
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
a typical signal sequence is 15-25 amino acids long, it has a tripartite structure consisting of a positively charged NH2-terminal region (n-region, 1-5 amino acids), a central hydrophobic core (h-region, 7-15 amino acids) probably arranged in a alpha-helix, and, separated by an alpha-helix breaking Pro or Gly, the more polar part (c-region, 3-7 amino acids), representing half of the cleavage site
-
-
?
additional information
?
-
uses a catalytic mechanism reminiscent of its eukaryal rather than its bacterial counterpart. The enzyme relies on a SerHisAsp catalytic triad
-
-
?
additional information
?
-
-
uses a catalytic mechanism reminiscent of its eukaryal rather than its bacterial counterpart. The enzyme relies on a SerHisAsp catalytic triad
-
-
?
additional information
?
-
uses a catalytic mechanism reminiscent of its eukaryal rather than its bacterial counterpart. The enzyme relies on a SerHisAsp catalytic triad
-
-
?
additional information
?
-
-
the enzyme is required for dislocation from the endoplasmic reticulium
-
-
?
additional information
?
-
-
the maturation of the core protein of hepatitis C virus is controlled by signal peptide peptidase Homo sapiens
-
-
?
additional information
?
-
-
signal peptide peptidase-catalysed liberation of mature core protein is absolutely dependent on prior cleavage by SP at the correct core-E1 site to generate the complete form of core protein
-
-
?
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
-
-
?
additional information
?
-
-
Inactivation of sipX does not effect intracellular multiplication of Listeria monocytogenes but significantly reduces bacterial virulence (about 100fold). Inactivation of sipZ impairs the secretion of phospholipase C and listeriolysin O, restricts intracellular multiplication and almost abolishes virulence. Inactivation of sipY has no detectable effects
-
-
?
additional information
?
-
-
signal peptidase I processes secretory signal sequences. The enzyme does not show a preference for the presence of acidic residues at second position of the mature protein (P2'). Substrate specificity and in silico prediction of signal peptidase I cleavage sites, overview
-
-
?
additional information
?
-
-
signal peptidase I processes secretory signal sequences. The enzyme does not show a preference for the presence of acidic residues at second position of the mature protein (P2'). Substrate specificity and in silico prediction of signal peptidase I cleavage sites, overview
-
-
?
additional information
?
-
-
GFP-tagged cleavage-site mutants are unstable compared with wild-type rem, suggesting improper folding
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
a typical signal sequence is 15-25 amino acids long, it has a tripartite structure consisting of a positively charged NH2-terminal region (n-region, 1-5 amino acids), a central hydrophobic core (h-region, 7-15 amino acids) probably arranged in a alpha-helix, and, separated by an alpha-helix breaking Pro or Gly, the more polar part (c-region, 3-7 amino acids), representing half of the cleavage site
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
a typical signal sequence is 15-25 amino acids long, it has a tripartite structure consisting of a positively charged NH2-terminal region (n-region, 1-5 amino acids), a central hydrophobic core (h-region, 7-15 amino acids) probably arranged in a alpha-helix, and, separated by an alpha-helix breaking Pro or Gly, the more polar part (c-region, 3-7 amino acids), representing half of the cleavage site
-
-
?
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
-
?
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
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
a typical signal sequence is 15-25 amino acids long, it has a tripartite structure consisting of a positively charged NH2-terminal region (n-region, 1-5 amino acids), a central hydrophobic core (h-region, 7-15 amino acids) probably arranged in a alpha-helix, and, separated by an alpha-helix breaking Pro or Gly, the more polar part (c-region, 3-7 amino acids), representing half of the cleavage site
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
a typical signal sequence is 15-25 amino acids long, it has a tripartite structure consisting of a positively charged NH2-terminal region (n-region, 1-5 amino acids), a central hydrophobic core (h-region, 7-15 amino acids) probably arranged in a alpha-helix, and, separated by an alpha-helix breaking Pro or Gly, the more polar part (c-region, 3-7 amino acids), representing half of the cleavage site
-
-
?
additional information
?
-
-
in addition to its catalysis of the cleavage of intermembrane space sorting signal Imp2p is required for the stable and functional expression of Imp1p
-
-
?
additional information
?
-
-
subunits Imp1p and Imp2p have separate, nonoverlapping substrate specificities
-
-
?
additional information
?
-
signal peptidase I processes secretory signal sequences. The enzyme does not show a preference for the presence of acidic residues at second position of the mature protein (P2'). Substrate specificity and in silico prediction of signal peptidase I cleavage sites, overview
-
-
?
additional information
?
-
-
signal peptidase I processes secretory signal sequences. The enzyme does not show a preference for the presence of acidic residues at second position of the mature protein (P2'). Substrate specificity and in silico prediction of signal peptidase I cleavage sites, overview
-
-
?
additional information
?
-
signal peptidase I processes secretory signal sequences. The enzyme does not show a preference for the presence of acidic residues at second position of the mature protein (P2'). Substrate specificity and in silico prediction of signal peptidase I cleavage sites, overview
-
-
?
additional information
?
-
-
in vitro preprotein processing by SpsB, overview. SpsB undergoes self-cleavage and, although the catalytic serine is retained in the self-cleavage product, a very low residual enzymatic activity remains. Self-cleavage at one amino acid before the catalytic serine
-
-
?
additional information
?
-
-
the enzyme shows a unique Ser/Lys dyad protease mechanism
-
-
?
additional information
?
-
-
identification of 46 proteins whose extracellular accumulation requires signal peptidase activity. Forty-four possess identifiable Sec-type signal peptides and thus are likely canonically secreted proteins, while four also appear to possess cell wall retention signals. For three proteins, HtrA, PrsA, and SAOUHSC_01761, secretion is induced by inhibitor arylomycin treatment
-
-
?
additional information
?
-
-
identification of 46 proteins whose extracellular accumulation requires signal peptidase activity. Forty-four possess identifiable Sec-type signal peptides and thus are likely canonically secreted proteins, while four also appear to possess cell wall retention signals. For three proteins, HtrA, PrsA, and SAOUHSC_01761, secretion is induced by inhibitor arylomycin treatment
-
-
?
additional information
?
-
-
the enzyme cleaves off the signal peptide from secreted proteins, making it essential for protein secretion, and hence for bacterial cell viability
-
-
?
additional information
?
-
-
isozyme Sip1 lacks the catalytic lysine. Development of fluorogenic peptide substrates, protease substrates containing a fluorescent donor chromophore and a quenching acceptor chromophore on either side of the enzyme cleavage site, whose fluorescence is quenched by intramolecular resonance energy transfer, FRET, between donor and a cceptor until the substrate is cleaved by the enzyme allowing continuous measurements, method development and evaluation, overview
-
-
?
additional information
?
-
-
measurement of enzyme activity using fluorescence resonance energy transfer-based assay
-
-
?
additional information
?
-
-
identification of 11 proteins whose secretion from stationary-phase Staphylococcus epidermidis is dependent on SPase activity. 9 of these are predicted to be translated with canonical N-terminal signal peptides. The presence of extracellular domains of lipoteichoic acid synthase and the beta-lactam response sensor BlaR1 in the medium is dependent on SPase activity, suggesting that they are cleaved at noncanonical sites within the protein
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
precursor of beta-lactamase and pre-OmpA fusion protein are no substrates, incubation at 37°C results in self-cleavage and appearance of 2 products with molecular masses of 19 kDa and 8 kDa
-
?
additional information
?
-
-
precursor of beta-lactamase and pre-OmpA fusion protein are no substrates, incubation at 37°C results in self-cleavage and appearance of 2 products with molecular masses of 19 kDa and 8 kDa
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
signal peptidase I processes secretory signal sequences. The enzyme does not show a preference for the presence of acidic residues at second position of the mature protein (P2'). Substrate specificity and in silico prediction of signal peptidase I cleavage sites, overview
-
-
?
additional information
?
-
-
signal peptidase I processes secretory signal sequences. The enzyme does not show a preference for the presence of acidic residues at second position of the mature protein (P2'). Substrate specificity and in silico prediction of signal peptidase I cleavage sites, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
core protein of classical swine fever virus + H2O
?
-
the processing of core protein of classical swine fever virus is conducted by signal peptide peptidase. Inhibition of this enzyme results in a reduced virus yield
-
-
?
hepatitis C virus core protein + H2O
?
-
signal peptide peptidase-catalyzed cleavage of hepatitis C virus core protein is dispensable for virus budding, but destabilizes the viral capsid
-
-
?
intermediate of cytochrome c peroxidase + H2O
mature cytochrome c peroxidase + peptide
-
Pcp1 is involved in processing of the intermediate of cytochrome c peroxidase
-
-
?
pre-SceD protein + H2O
SceD + presequence of pre-SceD
-
substrate of Sip2 and Sip3
-
-
?
signal peptides from preproteins + H2O
mature proteins
streptokinase precursor + H2O
streptokinase
additional information
?
-
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
in vivo, type I signal peptidase is the principal peptidase responsible for signal peptide cleavage as pre-proteins of a number of exported proteins, proteins designed for transport across the cytoplasmic membrane are generally synthesised as precursors with cleavable signal peptides in the cytoplasm, the signal peptides targets the pre-proteins to the respective translocase, during or shortly after translocation across the cytoplasmic membrane, the signal peptide is enzymatically removed
-
?
signal peptides from preproteins + H2O
mature proteins
-
in vivo, type I signal peptidase is the principal peptidase responsible for signal peptide cleavage as pre-proteins of a number of exported proteins, proteins designed for transport across the cytoplasmic membrane are generally synthesised as precursors with cleavable signal peptides in the cytoplasm, the signal peptides targets the pre-proteins to the respective translocase, during or shortly after translocation across the cytoplasmic membrane, the signal peptide is enzymatically removed
-
?
signal peptides from preproteins + H2O
mature proteins
-
in vivo, type I signal peptidase is the principal peptidase responsible for signal peptide cleavage as pre-proteins of a number of exported proteins, proteins designed for transport across the cytoplasmic membrane are generally synthesised as precursors with cleavable signal peptides in the cytoplasm, the signal peptides targets the pre-proteins to the respective translocase, during or shortly after translocation across the cytoplasmic membrane, the signal peptide is enzymatically removed
-
?
signal peptides from preproteins + H2O
mature proteins
-
key role in the protein secretary pathway
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
-
-
-
?
streptokinase precursor + H2O
streptokinase
-
extracellular protein, produced in pathogenic streptococci
-
?
streptokinase precursor + H2O
streptokinase
-
prestreptokinase is the native substrate, to be cleaved between Ala26 and Ile27
-
?
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
-
-
?
additional information
?
-
-
the enzyme is responsible for the full maturation of Toc75, the protein translocation channel at the plastid outer envelope membrane. the enzyme is required for biogenesis of plastid internal membranes
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
the physiological role is to release exported proteins from the membrane by removing the leader sequence
-
-
?
additional information
?
-
-
the enzyme removes amino-terminal leader peptides from exported proteins after they have crossed the plasma membrane
-
-
?
additional information
?
-
-
in addition to naturally occuring precursor protein substrates, signal peptidase can process short, synthetic peptide substrates based on the cleavage site region of pre-maltose binding protein and M13 procoat, minimum length for cleavage of peptide substrates is 5 residues, -3 to + 2 of the pre-maltose binding protein, indicating that the recognition sequence for signal peptidase lies between the -3 and +2 position
-
?
additional information
?
-
-
the physiological role is to release exported proteins from the membrane by removing the leader sequence
-
-
?
additional information
?
-
-
the enzyme is required for dislocation from the endoplasmic reticulium
-
-
?
additional information
?
-
-
the maturation of the core protein of hepatitis C virus is controlled by signal peptide peptidase Homo sapiens
-
-
?
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
-
-
?
additional information
?
-
-
Inactivation of sipX does not effect intracellular multiplication of Listeria monocytogenes but significantly reduces bacterial virulence (about 100fold). Inactivation of sipZ impairs the secretion of phospholipase C and listeriolysin O, restricts intracellular multiplication and almost abolishes virulence. Inactivation of sipY has no detectable effects
-
-
?
additional information
?
-
-
the enzyme cleaves off the signal peptide from secreted proteins, making it essential for protein secretion, and hence for bacterial cell viability
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3S)-3-((1R)-1-[(N-decanoyl-L-prolyl-L-threonyl-L-alanyl-L-asparaginyl)amino]ethyl)azetidin-2-one
-
beta-lactam lipopeptide, 57% inhibition at 0.1 mM
(3S)-3-((1S)-1-[(N-decanoyl-L-prolyl-L-threonyl-L-alanyl-L-asparaginyl)amino]ethyl)azetidin-2-one
-
beta-lactam lipopeptide, 47% inhibition at 0.1 mM
(5S,6S) penem
-
beta-lactam inhibitor
(5S,6S)-3-[(2-aminoethyl)sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-3-[[2-(carbamoyloxy)ethyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-3-[[2-(dimethylamino)ethyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-3-[[3-(dimethylcarbamoyl)cyclopentyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-[(2-hydroxyethyl)sulfanyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-[[2-(methylamino)ethyl]sulfanyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(1R)-3-oxocyclopentyl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(3R)-pyrrolidin-3-yl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(3S)-pyrrolidin-3-yl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[2-(pyridin-2-yl)ethyl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-6-[(2R)-2-hydroxypropyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
(5S,6S)-6-[(R)-acetoxyethyl]-penem-3-carboxylate
-
-
(NO2)YFSASALA
-
product inhibition
(Z-LL)2-ketone
-
completely abolishes signal peptide peptidase-catalysed maturation of p23 to p21 in the case of wild-type
1,3-bis[(N-benzyloxycarbonyl-L-leucyl-leucyl)amino]acetone
-
-
1-(2,5-dichlorophenyl)-3-(dimethylamino)propan-1-one
overexpression of lepB reduces the susceptibility of Mycobacterium tuberculosis to 1-(2,5-dichlorophenyl)-3-(dimethylamino)propan-1-one, and downregulation results in increased susceptibility. Treatment with 1-(2,5-dichlorophenyl)-3-(dimethylamino)propan-1-one leads to a rapid loss of viability and cell lysis. The compound has increased potency in nonreplicating cells, causing a reduction in viable cell numbers below the detection limit after 24 h
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
-
23 residue synthetic signal peptide of the M13 coat protein
-
-
-
4-nitrobenzyl (5S,6S)-6-(1-hydroxyethyl)-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-(acetyloxy)ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-(butanoyloxy)ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-(ethoxymethoxy)ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-(methoxymethoxy)ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(2-methylbutanoyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(2-methylpropanoyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(acetyloxy)methoxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(ethylcarbamoyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(N-acetylalanyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(N-acetylglycyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(N-acetylisoleucyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-6-[(1R)-1-[(N-acetylvalyl)oxy]ethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-7-oxo-6-[(1R)-1-(propanoyloxy)ethyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
4-nitrobenzyl (5S,6S)-7-oxo-6-[(1R)-1-[(propan-2-ylcarbamoyl)oxy]ethyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
5S penem derivative
-
best inhibitor
-
BAL0019193
a morpholino-beta-sultam derivative, inhibits SPase I by binding to non-overlapping subsites near the catalytic center in a noncovalent manner, binding mode, overview
benzyl (2S,5R,6S)-6-[(N-decanoyl-L-prolyl-L-threonyl-L-alanyl-L-asparaginyl)amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]-heptane-2-carboxylate
-
beta-lactam lipopeptide, 36% inhibition at 0.1 mM
Bromosuccinimide
-
inactivation by modification of tryptophan residues 300 and 310
Carboxyphenanthroline
-
-
Ciprofloxacin
-
1-cyclopropyl-6-fluoro-4-oxo-7-piperazin-1-ylquinoline-3-carboxylic acid
decanoyl-AKAPSKIDD
-
complete inhibition at 0.2 mM
decanoyl-L-prolyl-L-threonyl-L-alanyl-L-asparaginyl-carboxamide
-
beta-lactam lipopeptide, 60% inhibition at 100 mM, removal of the beta-lactam moiety results in a loss of activity
decanoyl-LTPTA
-
susceptible to classic protease inhibition, SpsB can be inhibited with a P1' proline
decanoyl-LTPTAKAPS
-
7.1% inhibition at 0.2 mM
diisopropyl fluorophosphate
-
partial inhibition
EDTA
-
mitochondrial Imp1p
L685,458
-
exerts only a slight effect on signal peptide peptidase-catalysed maturation of p23 to p21 in the case of wild-type, but it almost completely abolishes this process in the case of the Con1/C3/VLV replicon
lactacystin
-
proteasome inhibitor, presence in cells infected with mouse mammary tumor virus results in accumulation of uncleaved Rem relative to SP, consistent with SP retrotranslocation and proteasome escape before nuclear entry
Leader peptide of bacteriophage procoat
-
inhibits cleavage of M13 procoat or pre-maltose-binding protein
-
LTPTAKAPSKIDD
-
21.6% inhibition at 0.2 mM
MG132
-
proteasome inhibitor, presence in cells infected with mouse mammary tumor virus results in accumulation of uncleaved Rem relative to SP, consistent with SP retrotranslocation and proteasome escape before nuclear entry
N-hexadecanoyl-N-methylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-(13-methyltetradecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-(14-methylpentadecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-(14-methylpentadecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-pentadecanoylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-methyl-N-tetradecanoylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
N-[(1S)-1-(chloroacetyl)-3-methylbutyl]-4-methylbenzenesulfonamide
-
total loss of enzyme activity
N-[(2S)-4-[(2S)-1-decanoylpyrrolidin-2-yl]-2-(1-hydroxyethyl)-4-oxobutanoyl]-L-alanyl-N1-[(2S)-1-oxopropan-2-yl]-L-aspartamide
-
i.e. decanoyl-PTANA-aldehyde, inhibition by the synthetic substrate-based peptide aldehyde, overview. The length of the core lipopeptide can be reduced by removing several amino acids from both termini. Conversion of this peptide to an aldehyde. The signal peptide consists of three domains, a positively charged N-terminal domain, n-region, a hydrophobic middle domain, which contains usually 7-15 amino acids forming an alpha-helix, h-region, and a C-terminal domain, c-region, which is responsible for substrate recognition
phenylmethyl sulfonyl fluoride
-
partial inhibition
pre-protein including a proline at the +1 position
-
not cleaved, act as competitive inhibitors
-
prop-2-en-1-yl (5S,6S)-6-[(2R)-2-hydroxypropyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
Signal peptides that include a Pro residue at position +1
-
-
-
sodium chloride
-
above 160 mM
Synthetic leader peptide
-
-
-
(5S,6S)-3-[(2-aminoethyl)sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00063 mg/l
(5S,6S)-3-[(2-aminoethyl)sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-3-[(2-aminoethyl)sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-3-[[2-(carbamoyloxy)ethyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00096 mg/l
(5S,6S)-3-[[2-(carbamoyloxy)ethyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-3-[[2-(carbamoyloxy)ethyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-3-[[2-(dimethylamino)ethyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00395 mg/l
(5S,6S)-3-[[2-(dimethylamino)ethyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-3-[[2-(dimethylamino)ethyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-3-[[3-(dimethylcarbamoyl)cyclopentyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00122 mg/l
(5S,6S)-3-[[3-(dimethylcarbamoyl)cyclopentyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-3-[[3-(dimethylcarbamoyl)cyclopentyl]sulfanyl]-6-[(1R)-1-hydroxyethyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00104 mg/l
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-[(2-hydroxyethyl)sulfanyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00149 mg/l
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-[(2-hydroxyethyl)sulfanyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-[(2-hydroxyethyl)sulfanyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-[[2-(methylamino)ethyl]sulfanyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00637 mg/l
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-[[2-(methylamino)ethyl]sulfanyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-3-[[2-(methylamino)ethyl]sulfanyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(1R)-3-oxocyclopentyl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00116 mg/l
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(1R)-3-oxocyclopentyl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(1R)-3-oxocyclopentyl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(3R)-pyrrolidin-3-yl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00175 mg/l
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(3R)-pyrrolidin-3-yl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(3R)-pyrrolidin-3-yl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(3S)-pyrrolidin-3-yl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00080 mg/l
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(3S)-pyrrolidin-3-yl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[(3S)-pyrrolidin-3-yl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[2-(pyridin-2-yl)ethyl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00131 mg/l
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[2-(pyridin-2-yl)ethyl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(1R)-1-hydroxyethyl]-7-oxo-3-[[2-(pyridin-2-yl)ethyl]sulfanyl]-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(2R)-2-hydroxypropyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
IC50 is 0.00299 mg/l
(5S,6S)-6-[(2R)-2-hydroxypropyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
(5S,6S)-6-[(2R)-2-hydroxypropyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
-
-
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
-
arylomycin
A0A1S0QR24
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
arylomycin A-C16
-
inhibition of enzyme results in an insufficient flux of proteins through the secretion pathway leading to mislocalization of proteins. Inhibition results in synergistic sensitivity when combined with an aminoglycoside
arylomycin A-C16
-
inhibition of enzyme results in an insufficient flux of proteins through the secretion pathway leading to mislocalization of proteins. Inhibition results in synergistic sensitivity when combined with an aminoglycoside
arylomycin A-C16
-
secretion of proteins HtrA, PrsA, and SAOUHSC_01761 is induced by inhibitor treatment
arylomycin A-C16
-
Yersinia pestis strain KIM6+, unlike most Enterobacteriaceae, is susceptible to the arylomycins, a class of natural-product lipopeptide antibiotics that inhibit signal peptidase I (SPase). The arylomycin activity is conserved against a broad range of Yersinia pestis strains, overview. Alterations to each component of the Yersinia pestis lipopolysaccharide (O antigen, core, and lipid A) make at most only a small contribution to the unique sensitivity against arylomycin, also an increased affinity of the Yersinia pestis SPase for the antibiotic is not detected. Instead, the origins of the sensitivity can be traced to an increased dependence on SPase activity that results from high levels of protein secretion under physiological conditions. Deletion of the gene encoding the highly expressed cell adhesion protein Ail (locus tag y1324, UniProt ID Q8D0Z7) significantly alleviates sensitivity and overexpression of Ail or Escherichia coli maltose-binding protein then restores sensitivity, the arylomycin susceptibility of Yersinia pestis results from a temperature-dependent increase in protein secretion
arylomycin A2
0.01 mM, 90% inhibition
arylomycin A2
a lipohexapeptide-based natural product, inhibits SPase I by binding to non-overlapping subsites near the catalytic center in a noncovalent manner, binding mode, overview
arylomycin A2
-
a lipohexapeptide SPase I inhibitor, complete inhibition of each of the isozymes at 0.0002 mM by 0.00625 mM inhibitor
arylomycin A2
-
a lipohexapeptide SPase I inhibitor
dinitrophenol
-
-
dithiothreitol
90% inhibition. Enzyme contains a redox-active Cys pair and requires disulfide bond formation between them for its activity in vitro
N-hexadecanoyl-N-methylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
IC50: 190 nM
N-hexadecanoyl-N-methylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
IC50: 110 nM
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
IC50: 110 nM
N-methyl-N-(12-methyltridecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
N-methyl-N-(13-methyltetradecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
IC50: 130 nM
N-methyl-N-(13-methyltetradecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
N-methyl-N-(14-methylpentadecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
IC50: 130 nM
N-methyl-N-(14-methylpentadecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
N-methyl-N-(14-methylpentadecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
IC50: 170 nM
N-methyl-N-(14-methylpentadecanoyl)serylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-4,18-dihydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
N-methyl-N-pentadecanoylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
IC50: 130 nM
N-methyl-N-pentadecanoylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
N-methyl-N-tetradecanoylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
IC50: 110 nM
N-methyl-N-tetradecanoylserylalanyl-N-[13-carboxy-3-[(6-deoxyhexopyranosyl)oxy]-18-hydroxy-10-methyl-8,11-dioxo-9,12-diazatricyclo[13.3.1.12,6]icosa-1(19),2(20),3,5,15,17-hexaen-7-yl]-N-methylglycinamide
-
-
NEM
-
leader peptidase produced by replacing Ser90 with Cys
prop-2-en-1-yl (5S,6S)-6-[(2R)-2-hydroxypropyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
crystal structure of enzyme-bound 1, PDB ID 1B12
prop-2-en-1-yl (5S,6S)-6-[(2R)-2-hydroxypropyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
prop-2-en-1-yl (5S,6S)-6-[(2R)-2-hydroxypropyl]-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
-
-
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
A0A1S0QR24
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
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 any commercially available peptidase inhibitor including o-phenanthroline, ethylenediamine tetraacetic acid, phosphoramidon, 2,6-pyridine dicarboxylic acid, bestatin, tosyl-amido-2-phenylethyl chloromethyl ketone, 1-chloro-3-tosylamido-7-amino-2-heptanone hydrochloride, phenylmethylsulfonyl fluoride, 4-(amidinophenyl)methanesulfonyl fluoride, N-carbobenzyloxy-L-phenylalanyl chloromethyl ketone, dichloroisocoumarin, elastatinal, aprotinin, chymostatin, leupeptin, antipain dihydrochloride, iodoacetamide, N-ethylmaleimide, L-trans-epoxysuccinyl-leucylamido (4-guanidino) butane, 1,2-epoxy-3-(p nitrophenoxy)propane, pepstatin, and diaxoacetyl-DL-norleucine methyl ester
-
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
-
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
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
-
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
-
but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity; unaffected by inhibitors of most serine peptidases
-
additional information
-
but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity
-
additional information
-
but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity
-
additional information
-
not inhibited by classical protease inhibitors such as phenylmethyl sulfonyl fluoride, tosyl-amido-2-phenylethylchloromethylketone, EDTA, o-phenanthroline, N-ethylmaleimide, dinitrophenol, carboxyphenanthroline, or 2,6-pyridinecarboxylic acid
-
additional information
-
Ser90 and Asp153 are essential for catalysis
-
additional information
-
a mutant maltose-binding protein species with Pro at the +1 position interferes with the activity of signal peptidase in vivo, the mutant protein is not processed at either the normal site or an upstream alternate site previously identified, induced synthesis of this protein is inhibitory to cell growth and causes a pleiotrophic defect in processing of all nonlipoprotein precursors examined
-
additional information
-
-
-
additional information
-
scarcely inhibited by treatment with: N-acetylimidazole, iodoacetic acid, 5,5'-dithiobis(2-nitrobenzoic acid), succinic anhydride, 2,4,6-trinitrobenzenesulfonate
-
additional information
-
not inhibited by any commercially available peptidase inhibitor including o-phenanthroline, ethylenediamine tetraacetic acid, phosphoramidon, 2,6-pyridine dicarboxylic acid, bestatin, tosyl-amido-2-phenylethyl chloromethyl ketone, 1-chloro-3-tosylamido-7-amino-2-heptanone hydrochloride, phenylmethylsulfonyl fluoride, 4-(amidinophenyl)methanesulfonyl fluoride, N-carbobenzyloxy-L-phenylalanyl chloromethyl ketone, dichloroisocoumarin, elastatinal, aprotinin, chymostatin, leupeptin, antipain dihydrochloride, iodoacetamide, N-ethyl maleimide, L-trans-epoxysuccinyl-leucylamido (4-guanidino) butane, 1,2-epoxy-3-(p nitrophenoxy)propane, pepstatin, and diaxoacetyl-DL-norleucine methyl ester
-
additional information
beta-lactam antibiotics, one of the most important class of human therapeutics, act via the inhibition of penicillin-binding proteins (PBPs). Bacterial type I signal peptidase is evolutionarily related to the PBPs, but the stereochemistry of its substrates and its catalytic mechanism suggest that beta-lactams with the 5S stereochemistry, as opposed to the 5R stereochemistry of the traditional beta-lactams, are required for inhibition. Synthesis and evaluation of a variety of 5S penem derivatives and identify several with promising activity against both a Gram-positive and a Gram-negative bacterial pathogen, overview. The 5S beta-lactams possess significant antibacterial 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
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
-
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
-
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
-
a substrate based peptide aldehyde inhibits signal peptidases with a lower IC(50) value than other lipopeptides
-
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
-
inhibition by a synthetic substrate-based peptide aldehyde with IC50 of 0.009 mM and 0.013 mM for Sip2 and Sip3, respectively
-
additional information
-
beta-lactam antibiotics, one of the most important class of human therapeutics, act via the inhibition of penicillin-binding proteins (PBPs). Bacterial type I signal peptidase is evolutionarily related to the PBPs, but the stereochemistry of its substrates and its catalytic mechanism suggest that beta-lactams with the 5S stereochemistry, as opposed to the 5R stereochemistry of the traditional beta-lactams, are required for inhibition. Synthesis and evaluation of a variety of 5S penem derivatives and identify several with promising activity against both a Gram-positive and a Gram-negative bacterial pathogen, overview. The 5S beta-lactams possess significant antibacterial activity, MIC values against Staphylococcus epidermidis, overview
-
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
-
synthesis of a 5S penem from 6-aminopenicillanic acid, structure-activity relationships, overview
-
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
-
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
-
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
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
-
beta-lactam antibiotics, one of the most important class of human therapeutics, act via the inhibition of penicillin-binding proteins (PBPs). Bacterial type I signal peptidase is evolutionarily related to the PBPs, but the stereochemistry of its substrates and its catalytic mechanism suggest that beta-lactams with the 5S stereochemistry, as opposed to the 5R stereochemistry of the traditional beta-lactams, are required for inhibition. Synthesis and evaluation of a variety of 5S penem derivatives and identify several with promising activity against both a Gram-positive and a Gram-negative bacterial pathogen, overview. The 5S beta-lactams possess significant antibacterial activity, MIC values against Yersinia pestis, overview
-
additional information
-
strain identifiers and MIC values of arylomycin A-C16 and ciprofloxacin for the 30-member Yersinia pestis panel, overview. The MIC values increase with decreasing temperature
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
evolution
-
bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
evolution
-
bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
evolution
bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
evolution
-
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
evolution
-
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
evolution
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
evolution
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad. Bacillus subtilis contains five chromosomally encoded signal peptidases
evolution
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I that contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
evolution
evolutionary adaptation from the ribosome-dependent co-translational insertion to the chaperone-dependent post-translational transport of SPase I
evolution
-
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad. Bacillus subtilis contains five chromosomally encoded signal peptidases
-
evolution
-
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
-
evolution
-
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
-
evolution
-
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
-
evolution
-
bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
-
evolution
-
bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
-
evolution
-
bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
-
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
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
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
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
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
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
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
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
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
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
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
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
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
malfunction
A0A1S0QR24
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
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
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
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
malfunction
Staphylococcus aureus bacteria lacking the SPase I SpsB are viable and able to grow in vitro when overexpressing a native gene cassette encoding for a putative ABC transporter. This transporter apparently compensates for SpsB's essential function by mediating alternative cleavage of a subset of proteins at a site distinct from the SpsB-cleavage site, leading to SpsB-independent secretion
malfunction
the biofilm mutant, DELTASSA_0351, is deficient in type I signal peptidase (SPase), phenotype, overview. Proteomic analysis of mutant strain DELTASSA_0351, list of transcripts that are differentially regulated in DELTASSA_0351
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
-
malfunction
-
the biofilm mutant, DELTASSA_0351, is deficient in type I signal peptidase (SPase), phenotype, overview. Proteomic analysis of mutant strain DELTASSA_0351, list of transcripts that are differentially regulated in DELTASSA_0351
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
bacterial SPases I play a key role in protein secretion as they are responsible for the cleavage of signal peptides from secreted proteins
physiological function
-
Plsp1 is vital for proper thylakoid development in Arabidopsis thaliana chloroplasts. Plsp1 is also necessary for processing of an envelope protein, Toc75, and a thylakoid lumenal protein, OE33
physiological function
-
SPase I is responsible for removing the signal peptide from secretory pre-proteins and releasing mature proteins to cellular or extra-cellular space. SPase I may have an important role in Leishmania infectivity, e.g. in differentiation and survival of amastigotes
physiological function
-
the enzyme cleaves off the signal peptide from secreted proteins, making it essential for protein secretion, and hence for bacterial cell viability
physiological function
-
deletion of membrane-bound signal peptidases SipX, SipY and SipZ and construction of SipX/SipY and SipY/SipZ double mutants. The amounts of listeriolysin O, phosphatidylcholine phospholipase C and zinc metalloproteinase Mpl in the extracellular milieu are significantly decreased upon inactivation of SipZ. For the majority of the Sec-secreted exoproteins identified, protein secretion is not affected by the inactivation of one or two of the signal peptidases
physiological function
gene is essential for viability
physiological function
gene is essential, and reduced lepB expression is detrimental to growth
physiological function
RNAi-mediated knockdown of the catalytic subunit gene results in high mortality. Sixty-nine per cent of dead nymphs died of abnormal moulting, corresponding to decreased activity of moulting fluid protease. Insects in the RNAi group experience a decline in food intake, and a decrease in the secretion of total protein and digestive enzymes from midgut tissues to the midgut lumen. The females produce fewer eggs and eggs with disrupted embryogenesis
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
exported proteins require an N-terminal signal peptide to direct them from the cytoplasm to the periplasm. Once the protein has been translocated across the cytoplasmic membrane, the signal peptide is cleaved by a signal peptidase, allowing the remainder of the protein to fold into its mature state in the periplasm. Signal peptidase I (LepB) cleaves non-lipoproteins and recognises the sequence Ala-X-Ala. Amino acids present at the N-terminus of mature, exported proteins affect the efficiency at which the protein is exported
physiological function
involvement of signal peptidase I in Streptococcus sanguinis biofilm formation. Streptococcus sanguinis, a Gram-positive bacterium, is one of the most abundant species of the oral microbiota and it contributes to biofilm development in the oral cavity
physiological function
proteins that carry a type I signal peptide are released from their membrane anchored signal peptide by signal peptidase I (SPI). They can then remain in the periplasm, or be transported further. In Bacteroidetes, signal peptide cleavage exposes N-terminal glutamine residues in most signal peptidase I (SPI) substrates. The newly exposed glutamines are cyclized to pyroglutamate (also termed 5-oxoproline) residues. Porphyromonas gingivalis SPI substrates typically have a glutamine residue downstream of the SPI cleavage site. A Gln residue downstream of the SPI cleavage site affects RgpA, but not RgpB and Kgp gingipains secretion
physiological function
-
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
physiological function
-
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
physiological function
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
physiological function
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
physiological function
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
physiological function
type I signal peptidase (SPase I) mediates the final step of bacterial secretion, by cleaving proteins at their signal peptide once they are translocated by the Sec or twin-arginine (Tat) translocon. SPase I is important for viability in multiple bacterial pathogens. SpsB cleavage of the signal (or leader) peptide allows protein release from the membrane. A potential distinct secretion system involving an ABC transporter in Staphylococcus aureus is able to bypass the nominal essentiality of SpsB, overview
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
physiological function
A0A1S0QR24
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
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
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
-
physiological function
-
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
-
physiological function
-
involvement of signal peptidase I in Streptococcus sanguinis biofilm formation. Streptococcus sanguinis, a Gram-positive bacterium, is one of the most abundant species of the oral microbiota and it contributes to biofilm development in the oral cavity
-
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
-
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
-
physiological function
-
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
-
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
-
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
-
physiological function
-
SPase I is responsible for removing the signal peptide from secretory pre-proteins and releasing mature proteins to cellular or extra-cellular space. SPase I may have an important role in Leishmania infectivity, e.g. in differentiation and survival of amastigotes
-
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
-
physiological function
-
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
-
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
-
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
-
physiological function
-
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
-
physiological function
-
gene is essential, and reduced lepB expression is detrimental to growth
-
physiological function
-
proteins that carry a type I signal peptide are released from their membrane anchored signal peptide by signal peptidase I (SPI). They can then remain in the periplasm, or be transported further. In Bacteroidetes, signal peptide cleavage exposes N-terminal glutamine residues in most signal peptidase I (SPI) substrates. The newly exposed glutamines are cyclized to pyroglutamate (also termed 5-oxoproline) residues. Porphyromonas gingivalis SPI substrates typically have a glutamine residue downstream of the SPI cleavage site. A Gln residue downstream of the SPI cleavage site affects RgpA, but not RgpB and Kgp gingipains secretion
-
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
-
physiological function
-
proteins that carry a type I signal peptide are released from their membrane anchored signal peptide by signal peptidase I (SPI). They can then remain in the periplasm, or be transported further. In Bacteroidetes, signal peptide cleavage exposes N-terminal glutamine residues in most signal peptidase I (SPI) substrates. The newly exposed glutamines are cyclized to pyroglutamate (also termed 5-oxoproline) residues. Porphyromonas gingivalis SPI substrates typically have a glutamine residue downstream of the SPI cleavage site. A Gln residue downstream of the SPI cleavage site affects RgpA, but not RgpB and Kgp gingipains secretion
-
additional information
-
proper maturation of lumenal proteins may be a key process for correct assembly of thylakoids
additional information
if an N-terminal glutamine residue is exposed as a result of proteolysis, e.g. signal peptide proteolysis by signal peptidase 1, this glutamine residue has a tendency to cyclize to diglutamate, with release of ammonia as a side product. The transamidation reaction is thought to initiate with nucleophilic attack of the alpha-amino group on the carbonyl group of the side chain carboxamide, followed by collapse of the oxyanion intermediate and protonation of the leaving epsilon-amino group. Glutamine cyclization to diglutamate can occur spontaneously. The reaction is facilitated by inorganic catalysts such as phosphate ions serving as the proton shuttle, or can be catalyzed enzymatically by glutaminyl cyclases (QCs)
additional information
the energy requirement of integration of Plsp1 into isolated chloroplast membranes are satified by ATP hydrolysis. The C-terminal portion of Plsp1 including catalytic residues is predicted to form a hydrophobic surface at the trans-side of the membrane
additional information
-
the energy requirement of integration of Plsp1 into isolated chloroplast membranes are satified by ATP hydrolysis. The C-terminal portion of Plsp1 including catalytic residues is predicted to form a hydrophobic surface at the trans-side of the membrane
additional information
-
if an N-terminal glutamine residue is exposed as a result of proteolysis, e.g. signal peptide proteolysis by signal peptidase 1, this glutamine residue has a tendency to cyclize to diglutamate, with release of ammonia as a side product. The transamidation reaction is thought to initiate with nucleophilic attack of the alpha-amino group on the carbonyl group of the side chain carboxamide, followed by collapse of the oxyanion intermediate and protonation of the leaving epsilon-amino group. Glutamine cyclization to diglutamate can occur spontaneously. The reaction is facilitated by inorganic catalysts such as phosphate ions serving as the proton shuttle, or can be catalyzed enzymatically by glutaminyl cyclases (QCs)
-
additional information
-
if an N-terminal glutamine residue is exposed as a result of proteolysis, e.g. signal peptide proteolysis by signal peptidase 1, this glutamine residue has a tendency to cyclize to diglutamate, with release of ammonia as a side product. The transamidation reaction is thought to initiate with nucleophilic attack of the alpha-amino group on the carbonyl group of the side chain carboxamide, followed by collapse of the oxyanion intermediate and protonation of the leaving epsilon-amino group. Glutamine cyclization to diglutamate can occur spontaneously. The reaction is facilitated by inorganic catalysts such as phosphate ions serving as the proton shuttle, or can be catalyzed enzymatically by glutaminyl cyclases (QCs)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
12000
-
1 * 25000 + 1 * 22000-23000 (a glycoprotein) + 1 * 21000 + 1 * 18000 + 1 * 12000, dog, SDS-PAGE
20067
x * 20067, calculated
21500
-
his-tagged version, overexpressed in Escherichia coli, Western blotting
22000
-
deduced from DNA sequence
24600
-
deduced from DNA sequence
26380
-
mass spectrometry
268000
-
protease IV, gel filtration
27910
-
E. coli, detergent-free DELTA2-75 mutant protein lacking the two N-terminal transmembrane spanning and the cytoplasmic domains, calculation from amino acid sequence
30000
-
gel filtration, SDS-PAGE
32103
x * 32103, calculated
41000
x * 41000, calculated from sequence
42000
x * 42000, calculated from sequence
640000
-
protease IV, determined in presence of Triton X-100
67240
-
hypothetical polypeptide sequence deduced from the DNA sequence
13000
-
1 * 18000 + 1 * 20000 + 1 * 25000 + 1 * 13000 (the association of the 13000 MW protein with the enzymatic activity is tentative), yeast, SDS-PAGE
13000
-
1 * 18000 + 1 * 20000 + 1 * 25000 + 1 * 13000 (the association of the 13000 MW protein with the enzymatic activity is tentative), yeast, SDS-PAGE
13000
-
1 * 13000 + 1 * 18000 + 1 * 20000 + 1 * 25000
18000
-
1 * 25000 + 1 * 22000-23000 (a glycoprotein) + 1 * 21000 + 1 * 18000 + 1 * 12000, dog, SDS-PAGE
18000
-
1 * 18000 + 1 * 20000 + 1 * 25000 + 1 * 13000 (the association of the 13000 MW protein with the enzymatic activity is tentative), yeast, SDS-PAGE
18000
-
1 * 18000 + 1 * 20000 + 1 * 25000 + 1 * 13000 (the association of the 13000 MW protein with the enzymatic activity is tentative), yeast, SDS-PAGE
18000
-
1 * 13000 + 1 * 18000 + 1 * 20000 + 1 * 25000
19000
-
1 * 22000-23000 + 1 * 19000, chicken, SDS-PAGE
19000
-
1 * 22000-23000 + 1 * 19000, chicken, SDS-PAGE
19000
-
1 * 22000-23000 + 1 * 19000, chicken, SDS-PAGE
19000
-
1 * 22000-23000 + 1 * 19000, chicken, SDS-PAGE
19000
-
1 * 23000 + 1 * 19000, gp23 and p19
19000
-
1 * 23000 + 1 * 19000, gp23 and p19
20000
-
1 * 18000 + 1 * 20000 + 1 * 25000 + 1 * 13000 (the association of the 13000 MW protein with the enzymatic activity is tentative), yeast, SDS-PAGE
20000
-
1 * 18000 + 1 * 20000 + 1 * 25000 + 1 * 13000 (the association of the 13000 MW protein with the enzymatic activity is tentative), yeast, SDS-PAGE
20000
-
1 * 13000 + 1 * 18000 + 1 * 20000 + 1 * 25000
21000
-
deduced from DNA sequence
21000
-
deduced from DNA sequence
21000
-
deduced from DNA sequence
21000
-
deduced from DNA sequence
21000
-
deduced from DNA sequence
21000
-
1 * 25000 + 1 * 22000-23000 (a glycoprotein) + 1 * 21000 + 1 * 18000 + 1 * 12000, dog, SDS-PAGE
23000
-
1 * 23000 + 1 * 19000, gp23 and p19
23000
-
1 * 23000 + 1 * 19000, gp23 and p19
25000
-
1 * 25000 + 1 * 22000-23000 (a glycoprotein) + 1 * 21000 + 1 * 18000 + 1 * 12000, dog, SDS-PAGE
25000
-
1 * 18000 + 1 * 20000 + 1 * 25000 + 1 * 13000 (the association of the 13000 MW protein with the enzymatic activity is tentative), yeast, SDS-PAGE
25000
-
1 * 18000 + 1 * 20000 + 1 * 25000 + 1 * 13000 (the association of the 13000 MW protein with the enzymatic activity is tentative), yeast, SDS-PAGE
25000
-
1 * 13000 + 1 * 18000 + 1 * 20000 + 1 * 25000
25000
-
1 * 25000 + 1 * 22000-23000 + 21000 + 18000 + 12000, subunits are named SP25, SP22/23, SPC21, SPC18, and SPC12, SDS-PAGE
27950
-
E. coli detergent-free DELTA2-75 mutant protein lacking the two N-terminal transmembrane spanning and the cytoplasmic domains, electrospray ionization mass spectrometry
27950
-
deduced from amino acid sequence
32000
-
active monomer, SDS-PAGE
32000
-
deduced from DNA sequence
36000
-
active monomer, SDS-PAGE
37000
-
active monomer, SDS-PAGE
37000
-
1 * 37000, SDS-PAGE
37000
-
x * 37000, SDS-PAGE
37000
x * 37000, calculated from sequence
37000
-
x * 37000, wild-type and mutant enzymes, SDS-PAGE
48000
-
1 * 51000 + 1 * 48000, yeast, SDS-PAGE
48000
-
1 * 51000 + 1 * 48000, yeast, SDS-PAGE
48000
-
1 * 51000 + 1 * 48000, yeast, SDS-PAGE
48000
-
1 * 51000 + 1 * 48000, yeast, SDS-PAGE
51000
-
1 * 51000 + 1 * 48000, yeast, SDS-PAGE
51000
-
1 * 51000 + 1 * 48000, yeast, SDS-PAGE
51000
-
1 * 51000 + 1 * 48000, yeast, SDS-PAGE
51000
-
1 * 51000 + 1 * 48000, yeast, SDS-PAGE
52000
-
1 * 57000 + 1 * 52000, Neurospora crassa, SDS-PAGE
52000
-
1 * 57000 + 1 * 52000, Neurospora crassa, SDS-PAGE
52000
-
1 * 57000 + 1 * 52000, Neurospora crassa, SDS-PAGE
52000
-
1 * 57000 + 1 * 52000, Neurospora crassa, SDS-PAGE
52000
-
1 * 52000 + 1 * 55000, SDS-PAGE
52000
-
1 * 52000 + 1 * 55000, SDS-PAGE
52000
-
1 * 52000 + 1 * 55000, SDS-PAGE
52000
-
1 * 52000 + 1 * 55000, SDS-PAGE
55000
-
1 * 52000 + 1 * 55000, SDS-PAGE
55000
-
1 * 52000 + 1 * 55000, SDS-PAGE
55000
-
1 * 52000 + 1 * 55000, SDS-PAGE
55000
-
1 * 52000 + 1 * 55000, SDS-PAGE
57000
-
1 * 57000 + 1 * 52000, Neurospora crassa, SDS-PAGE
57000
-
1 * 57000 + 1 * 52000, Neurospora crassa, SDS-PAGE
57000
-
1 * 57000 + 1 * 52000, Neurospora crassa, SDS-PAGE
57000
-
1 * 57000 + 1 * 52000, Neurospora crassa, SDS-PAGE
60000
recombinant fusion protein MBP-SipS-P2
60000
recombinant fusion protein MBP-SipS-P2
63000
recombinant fusion protein MBP-SipS
63000
recombinant fusion protein MBP-SipS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S142A
very poor activity with PsbO substrate
D142E
10% of wild-type activity
D142I
as active as wild-type enzyme
D273A
-
site directed scanning mutagenesis
D273A/R146A
-
site directed scanning mutagenesis
D273A/R146A/T94V
-
site directed scanning mutagenesis
D273N
-
site directed scanning mutagenesis
D280A
-
site directed scanning mutagenesis
D280E
-
site directed scanning mutagenesis
F84A
50% of wild-type activity
F84W
10% of wild-type activity
G272A
-
site directed scanning mutagenesis
G278A
-
site directed scanning mutagenesis
G285A
-
site directed scanning mutagenesis
G89A
as active as wild-type enzyme
I130A
as active as wild-type enzyme
I144A
50% of wild-type activity
I144A/I86A
0.1% of wild-type activity
I144C
50% of wild-type activity, mutant enzyme cleaves at multiple sites
I144S
10% of wild-type activity
I86A
0.5% of wild-type activity
I86A/I144A
mutant enzyme is able to cleave after Phe at the -1 residue
L95A
10% of wild-type activity
M91A
5% of wild-type activity
N274A
-
site directed scanning mutagenesis
N277A
-
site directed scanning mutagenesis
N277D
-
site directed scanning mutagenesis
R146A
-
site directed scanning mutagenesis
R146M
-
site directed scanning mutagenesis
R222A
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value. Thermostability is significantly lower compared to the wild-type enzyme
R222K
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value. Thermostability is significantly lower compared to the wild-type enzyme
R282M
-
site directed scanning mutagenesis
R315A
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value. Thermostability is significantly lower compared to the wild-type enzyme
R318A
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value
R318K
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value. Thermostability is significantly lower compared to the wild-type enzyme
R77A
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value
R77K
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value
T94V
-
site directed scanning mutagenesis
T94V/R146A
-
site directed scanning mutagenesis
V132A
1% of wild-type activity
V132I
as active as wild-type enzyme
W261F/W284F/W300F
mutant based on deletion mutant DELTA2-75. Mutant contains one remaining Trp residue and is able to insert into lipids
W261F/W284F/W310F
mutant based on deletion mutant DELTA2-75. Mutant contains one remaining Trp residue and is able to insert into lipids
W261F/W300F/W310F
mutant based on deletion mutant DELTA2-75. Mutant contains one remaining Trp residue, its solvent accesibilities are modified in the presence of signal peptide
W284F/W300F/W310F
mutant based on deletion mutant DELTA2-75. Mutant contains one remaining Trp residue, its solvent accesibilities are modified in the presence of signal peptide
Y143A
10% of wild-type activity
Y143W
as active as wild-type enzyme
C51A
-
Lbpro mutant, site-directed mutagenesis
C51A/C133S
-
Lbpro-double mutant, site-directed mutagenesis
D187A
no catalytic activity
D187N
no catalytic activity
K115A
mutant is as active as the native enzyme
K79A
mutant is as active as the native enzyme
D187A
-
no catalytic activity
-
D187N
-
no catalytic activity
-
K115A
-
mutant is as active as the native enzyme
-
K79A
-
mutant is as active as the native enzyme
-
K174A
-
mutation is lethal
-
S94A
-
mutation is lethal
-
S96A
-
mutation is lethal
-
K76A
-
signal peptidase I, site-directed mutagenesis
S38A
-
signal peptidase I, site-directed mutagenesis
D215A
-
Vmax is 1.8fold lower than wild-type value, kcat is 1.8 fold lower than wild-type enzyme
D277A
-
Vmax is 1.6fold higher than wild-type value, kcat is 1.6fold higher than wild-type enzyme
E226A
-
Vmax is 1.35fold higher than wild-type value, kcat is 1.3fold higher than wild-type enzyme
E227A
-
Vmax is is nearly identical to wild-type value, kcat nearly identical to wild-type enzyme
H191A
-
Vmax is 1.84fold lower than wild-type value, kcat is 1.9fold lower than wild-type enzyme
K150A
-
Vmax is 1.5fold higher than wild-type value, kcat is 1.4fold higher than wild-type enzyme
K209A
-
Vmax is 1.7fold lower than wild-type value, kcat is 1.8fold lower than wild-type enzyme
R221A
-
Vmax is 7.8fold lower than wild-type value, kcat is 8fold lower than wild-type enzyme
R250A
-
Vmax is 1.5fold higher than wild-type value, kcat is 1.4fold higher than wild-type enzyme
S128A
-
Vmax is 6.9 fold higher than wild-type value, kcat is 6.2fold higher than wild-type enzyme
S184A
-
Vmax is 4fold lower than wild-type value, kcat is 4fold lower than wild-type enzyme
Y165A
-
Vmax is 2.3fold higher than wild-type value, kcat is 2.3fold higher than wild-type enzyme
P91S
-
construction of LepB(P91S) mutant strain DBS600 via allelic exchange and site-directed mutagenesis to introduce the point mutation. The mutant can be complemented by expression of wild-type SPase from Yersinia pestis or Escherichia coli
S36A
-
inactive
additional information
-
disruption of PLSP1 expression by a T-DNA insertion causes a seedling lethal phenotype in which development of internal membranes was severely retarded in cotyledon plastids. Construction of a plsp1-null mutant. Plastids that lack Plsp1 accumulate vesicles of variable sizes in the stroma, and they cause a reduction in accumulation of thylakoid proteins and that Plsp1 is involved in maturation of two additional lumenal proteins, OE23 and plastocyanin. OE33 associates with the stromal vesicles of the mutant plastids. Accumulation of improperly processed forms of Toc75 in the plastid envelope does not disrupt normal plant development, presence of posttranscriptional suppression of thylakoid protein accumulation in plsp1-1 plants, phenotype, overview
additional information
construction of a N-terminally truncated enzyme lacking amino acids 1-134 and a full-length mature form containing the trans-membrane domain but lacking the transit peptide. N-terminally truncated variant shows very poor activity with PsbO substrate
additional information
-
construction of a N-terminally truncated enzyme lacking amino acids 1-134 and a full-length mature form containing the trans-membrane domain but lacking the transit peptide. N-terminally truncated variant shows very poor activity with PsbO substrate
additional information
using a heterologous system, targeting of Arabidopsis thaliana Plsp1 to pea chloroplasts/chloroplast membranes is performed
additional information
-
using a heterologous system, targeting of Arabidopsis thaliana Plsp1 to pea chloroplasts/chloroplast membranes is performed
additional information
-
expression of a soluble form of signal peptidase, which lacks the two transmembrane domains, SPase I DELTA2-75
additional information
-
variant DELTA2-75 is a soluble form of signal peptidase, which lacks the two transmembrane domains
additional information
generation of a DELTA2-76 truncated enzyme mutant by deletion. The mutant is soluble and lacks both N-terminal transmembrane domains
additional information
-
generation of a DELTA2-76 truncated enzyme mutant by deletion. The mutant is soluble and lacks both N-terminal transmembrane domains
additional information
-
construction of a null mutant of SPase I is not possible, suggesting that SPase I is an essential gene for parasite survival. The obtained heterozygote mutant by disrupting one allele of SPase I show significantly reduced level of infectivity in bone marrow-derived macrophages. The heterozygote mutants are unable to cause cutaneous lesion in susceptible BALB/c mice. Comparison of in vivo infectivity potential of DELTAspase::NEO/SPase heterozygote mutant and wild-type parasites, overview
additional information
-
construction of a null mutant of SPase I is not possible, suggesting that SPase I is an essential gene for parasite survival. The obtained heterozygote mutant by disrupting one allele of SPase I show significantly reduced level of infectivity in bone marrow-derived macrophages. The heterozygote mutants are unable to cause cutaneous lesion in susceptible BALB/c mice. Comparison of in vivo infectivity potential of DELTAspase::NEO/SPase heterozygote mutant and wild-type parasites, overview
-
additional information
inactivation of sipM by targeted gene disruption cannot be achieved, indicating its essential role for cell viability
additional information
-
inactivation of sipM by targeted gene disruption cannot be achieved, indicating its essential role for cell viability
additional information
-
a truncated derivative of SpsB, which is nine amino acids longer at the N-terminus compared to the self-cleavage product, retains activity
additional information
generation of Staphylococcus aureus bacteria lacking the SPase I SpsB, KIM6+ phoP knockout strain
additional information
-
generation of Staphylococcus aureus bacteria lacking the SPase I SpsB, KIM6+ phoP knockout strain
additional information
generation of the biofilm mutant, DELTASSA_0351, that is deficient in type I signal peptidase (SPase). Although the growth curve of the DSSA_0351 mutant shows no significant difference from that of the wild-type strain SK36, biofilm assays using both microtitre plate assay and confocal laser scanning microscopy (CLSM) confirmed a sharp reduction in biofilm formation in the mutant compared to the wild-type strain and the paralogous mutant DSSA_0849. Evaluation of the functional impact of SPase on biofilm formation, transcriptome analysis compared to wild-type, overview. The growth rates of the wild-type, DSSA_0849 and DSSA_0351 strains are not significantly different. Proteomic analysis of mutant strain DELTASSA_0351, list of transcripts that are differentially regulated in DELTASSA_0351
additional information
-
generation of the biofilm mutant, DELTASSA_0351, that is deficient in type I signal peptidase (SPase). Although the growth curve of the DSSA_0351 mutant shows no significant difference from that of the wild-type strain SK36, biofilm assays using both microtitre plate assay and confocal laser scanning microscopy (CLSM) confirmed a sharp reduction in biofilm formation in the mutant compared to the wild-type strain and the paralogous mutant DSSA_0849. Evaluation of the functional impact of SPase on biofilm formation, transcriptome analysis compared to wild-type, overview. The growth rates of the wild-type, DSSA_0849 and DSSA_0351 strains are not significantly different. Proteomic analysis of mutant strain DELTASSA_0351, list of transcripts that are differentially regulated in DELTASSA_0351
additional information
-
generation of the biofilm mutant, DELTASSA_0351, that is deficient in type I signal peptidase (SPase). Although the growth curve of the DSSA_0351 mutant shows no significant difference from that of the wild-type strain SK36, biofilm assays using both microtitre plate assay and confocal laser scanning microscopy (CLSM) confirmed a sharp reduction in biofilm formation in the mutant compared to the wild-type strain and the paralogous mutant DSSA_0849. Evaluation of the functional impact of SPase on biofilm formation, transcriptome analysis compared to wild-type, overview. The growth rates of the wild-type, DSSA_0849 and DSSA_0351 strains are not significantly different. Proteomic analysis of mutant strain DELTASSA_0351, list of transcripts that are differentially regulated in DELTASSA_0351
-
additional information
-
a truncated protein without the N-terminal 54 residues and putative transmembrane domain, exhibits high peptidase activity, and is used as the wild-type protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
analysis
-
development of a fluorescence resonance energy transfer-based assay method as a rapid and reliable tool in future research for the identification and validation of potential SPase I inhibitors
drug development
-
type I signal peptidase is a potential target for the development of novel antibacterial agents
drug development
-
bacterial type I signal peptidase is a potential target for the development of antibacterial agents
drug development
-
in the search for antibacterial therapies, the type I signal peptidase serves as a potential target for development of antibacterials with another mode of action. SPase I is also is a feasible target for biofilm-associated infections
drug development
SPase I is a target for development of inhibitors as antibiotics
drug development
-
SPase I serves as a potentially interesting target for the development of antibacterials with another mode of action
drug development
-
bacterial signal peptidase I (SPase) is a target for development of beta-lactam anti-bacterial inhibitors
drug development
-
bacterial signal peptidase I (SPase) is a target for development of beta-lactam anti-bacterial inhibitors
drug development
bacterial signal peptidase I (SPase) is a target for development of beta-lactam anti-bacterial inhibitors
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
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
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
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
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
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
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
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
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
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
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
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
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
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
drug development
A0A1S0QR24
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
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
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
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
drug development
-
bacterial signal peptidase I (SPase) is a target for development of beta-lactam anti-bacterial inhibitors
-
drug development
-
bacterial signal peptidase I (SPase) is a target for development of beta-lactam anti-bacterial inhibitors
-
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
-
drug development
-
bacterial signal peptidase I (SPase) is a target for development of beta-lactam anti-bacterial inhibitors
-
medicine
-
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
medicine
-
inhibition of enzyme by arylomycin A-C16 results in an insufficient flux of proteins through the secretion pathway leading to mislocalization of proteins. Inhibition results in synergistic sensitivity of cells when combined with an aminoglycoside. Antibiotics tetracycline, erythromycin, and vancomycin each interact additively with arylomycin A-C16, while rifampin and trimethoprim show pronounced antagonism
medicine
-
inhibition of enzyme by arylomycin A-C16 results in an insufficient flux of proteins through the secretion pathway leading to mislocalization of proteins. Inhibition results in synergistic sensitivity of cells when combined with an aminoglycoside. No significant interactions are observed between arylomycin A-C16 and erythromycin, polymyxin B, trimethoprim, or ciprofloxacin. Arylomycin A-C16 shows mild synergism with cephalexin, pronounced synergism with rifampin and gentamicin, and antagonism with the translational inhibitor tetracycline
medicine
-
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
-
pharmacology
-
enzyme is essential for bacterial cell viability, potential molecular target for development of novel antibacterial agents
pharmacology
possible targets for the design of novel antibiotics
pharmacology
possible targets for the design of novel antibiotics
pharmacology
-
signal peptidase structure will be useful in the design of new and improved inhibitors which may be of pharmaceutical importance
pharmacology
-
signal peptidase structure will be useful in the design of new and improved inhibitors which may be of pharmaceutical importance
pharmacology
-
the gram positive pathogen plays a significant role in infectious disease, including life threatening methicillin-resistant MRSA infections, the ability to screen for inhibitors of SpsB will represent a significant advance for discovery of antibacterial agents