3.4.21.89: Signal peptidase I
This is an abbreviated version!
For detailed information about Signal peptidase I, go to the full flat file.
Word Map on EC 3.4.21.89
-
3.4.21.89
-
polyproteins
-
lipoprotein
-
preproteins
-
cleavable
-
foot-and-mouth
-
unprocessed
-
dyad
-
membrane-spanning
-
prolipoproteins
-
translocons
-
pilins
-
uncleaved
-
beta-lactamase
-
drug development
-
flavivirus
-
ompa
-
nonstructural
-
cotranslationally
-
co-translational
-
sec-dependent
-
globomycin
-
presequence
-
papain-like
-
prepeptide
-
polytopic
-
oligonucleotide-directed
-
ns2b
-
signal-anchored
-
pharmacology
-
medicine
-
analysis
- 3.4.21.89
- polyproteins
- lipoprotein
- preproteins
-
cleavable
- foot-and-mouth
-
unprocessed
-
dyad
-
membrane-spanning
- prolipoproteins
-
translocons
- pilins
-
uncleaved
- beta-lactamase
- drug development
- flavivirus
- ompa
-
nonstructural
-
cotranslationally
-
co-translational
-
sec-dependent
- globomycin
- presequence
-
papain-like
- prepeptide
-
polytopic
-
oligonucleotide-directed
- ns2b
-
signal-anchored
- pharmacology
- medicine
- analysis
Reaction
Cleavage of hydrophobic, N-terminal signal or leader sequences =
Synonyms
Bacterial leader peptidase 1, bacterial type I signal peptidase, big signal peptidase, canine signal peptidase complex, chloroplast processing peptidase, EC 3.4.99.36, Escherichia coli leader peptidase, Eukaryotic signal peptidase, Eukaryotic signal proteinase, hen oviduct signal peptidase, HOSP, imp1p, Leader peptidase, Leader peptidase I, Leader peptide hydrolase, Leader proteinase, LEP, LepB, PA1303, Pcp1, Peptidase, signal, Pilin leader peptidase, plastidic SPase I, plastidic SPase I 1, plastidic type I signal peptidase 1, Plsp1, Prokaryotic leader peptidase, Prokaryotic signal peptidase, Prokaryotic signal proteinase, Propeptidase, protease IV, Proteinase, eukaryotic signal, Proteinase, signal, PuIO prepilin peptidase, Rv2903c, SEC11, secretory protein 11, Signal peptidase, signal peptidase I, signal peptidase I-3, Signal peptidase IB, signal peptidase type I, Signal peptide hydrolase, Signal peptide peptidase, Signalase, Sip1, Sip2, Sip3, SipP (pTA1015), SipP (pTA1040), SipS, SipT, SipU, SipV, SipW, SipX, SipY, SipZ, SP, SP I, SP-I, SPase, Spase I, SPase I 1, SPase IB, SPaseI, SPC, Spc1, SPI, SPP, SpsB, thylakoidal processing peptidase, TPP, type I signal (leader) peptidase, type I signal peptidase, type I signal peptidase 1, type I signal peptidase Sec11a, type I signal peptidase Sec11b, type I SPase
ECTree
3.4.21.89 Signal peptidase IAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.89 - Signal peptidase I
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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-AGPRPTRIAFGA-NH2 + H2O
N-acetyl-L-alanine + GPRPTRIAFGA-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-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
-
-
?
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
-
-
?
envelope protein Toc75 precursor + H2O
mature envelope protein Toc75 + signal peptide
-
-
-
?
Eukaryotic initiation factor eIF-4gamma from rabbit reticulocytes + H2O
?
-
cleavage site Gly479-Arg480
-
-
?
hexanoyl-LTPTQAKAASKIDD-OH + H2O
hexanoyl-LTPTQAKA + ASKIDD
-
-
-
?
KLTFGTVKPVQAIAGYEWL + H2O
?
-
synthetic peptide substrate, based upon the signal peptide of prestreptokinase from Streptococcus pyogene
-
?
mammalian cytochrome b(5) precursor + H2O
?
the processing can occur after almost complete exocytoplasmic translocation of the preprotein is accomplished
-
-
?
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
-
?
octanoyl-LTPTQAKAASKIDD-OH + H2O
octanoyl-LTPTQAKA + ASKIDD
-
-
-
?
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
-
-
-
-
?
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 the 23kd photosystem II protein + H2O
23kd Photosystem II protein + ?
-
-
-
-
?
Precursors of the exported proteins Skp of E. coli + H2O
Exported proteins Skp of E. coli + ?
-
processed at the authentic site
-
-
?
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
-
-
?
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
-
?
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
-
-
?
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
-
?
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
-
-
-
?
(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
-
-
-
?
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
-
-
-
-
?
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
-
?
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-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
-
?
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
-
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
-
-
?
