Application | Comment | Organism |
---|---|---|
pharmacology | signal peptidase structure will be useful in the design of new and improved inhibitors which may be of pharmaceutical importance | Staphylococcus aureus |
pharmacology | signal peptidase structure will be useful in the design of new and improved inhibitors which may be of pharmaceutical importance | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
- |
Salmonella enterica subsp. enterica serovar Typhimurium |
- |
Gallus gallus |
- |
Haemophilus influenzae |
- |
Rattus norvegicus |
- |
Pseudomonas fluorescens |
- |
Canis lupus familiaris |
- |
Methanocaldococcus jannaschii |
- |
Rana sp. |
- |
Caenorhabditis elegans |
- |
Homo sapiens |
- |
Rhodobacter capsulatus |
- |
Schizosaccharomyces pombe |
19 kDa subunit encoded by SEC11 gene | Saccharomyces cerevisiae |
lepB gene cloned and sequenced | Escherichia coli |
Sec11 gene product identified as 18 kDa subunit, cloning of the gene encoding imp1p | Saccharomyces cerevisiae |
Crystallization (Comment) | Organism |
---|---|
- |
Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
23 residue synthetic signal peptide of the M13 coat protein | - |
Escherichia coli | |
5S penem derivative | best inhibitor | Escherichia coli | |
EDTA | mitochondrial Imp1p | Saccharomyces cerevisiae | |
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 | Bacillus subtilis | |
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 | Escherichia coli | |
pre-protein including a proline at the +1 position | not cleaved, act as competitive inhibitors | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0165 | - |
pro-ompA-nuclease | pH 8.0 | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Bacillus subtilis | 5737 | - |
cytoplasm | - |
Escherichia coli | 5737 | - |
cytoplasm | - |
Saccharomyces cerevisiae | 5737 | - |
endoplasmic reticulum | - |
Gallus gallus | 5783 | - |
microsome | - |
Gallus gallus | - |
- |
microsome | - |
Canis lupus familiaris | - |
- |
mitochondrion | mitochondrial inner membrane | Saccharomyces cerevisiae | 5739 | - |
plasma membrane | - |
Bradyrhizobium japonicum | 5886 | - |
plasma membrane | the active site o the enzyme is located in the periplasm | Escherichia coli | 5886 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
13000 | - |
1 * 13000 + 1 * 18000 + 1 * 20000 + 1 * 25000 | Saccharomyces cerevisiae |
18000 | - |
1 * 13000 + 1 * 18000 + 1 * 20000 + 1 * 25000 | Saccharomyces cerevisiae |
19000 | - |
1 * 23000 + 1 * 19000, gp23 and p19 | Gallus gallus |
20000 | - |
1 * 13000 + 1 * 18000 + 1 * 20000 + 1 * 25000 | Saccharomyces cerevisiae |
21000 | - |
deduced from DNA sequence | Staphylococcus aureus |
21000 | - |
deduced from DNA sequence | Bacillus subtilis |
21000 | - |
deduced from DNA sequence | Bacillus licheniformis |
21000 | - |
deduced from DNA sequence | Bacillus amyloliquefaciens |
21000 | - |
deduced from DNA sequence | [Bacillus] caldolyticus |
22000 | - |
deduced from DNA sequence | Phormidium laminosum |
23000 | - |
1 * 23000 + 1 * 19000, gp23 and p19 | Gallus gallus |
24000 | - |
- |
Methanocaldococcus jannaschii |
25000 | - |
1 * 13000 + 1 * 18000 + 1 * 20000 + 1 * 25000 | Saccharomyces cerevisiae |
25000 | - |
1 * 25000 + 1 * 22000-23000 + 21000 + 18000 + 12000, subunits are named SP25, SP22/23, SPC21, SPC18, and SPC12, SDS-PAGE | Canis lupus familiaris |
32000 | - |
deduced from DNA sequence | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | 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 | ? | - |
? | |
signal peptides from preproteins + H2O | Salmonella enterica subsp. enterica serovar Typhimurium | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Gallus gallus | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Staphylococcus aureus | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Haemophilus influenzae | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Bacillus subtilis | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Rattus norvegicus | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Saccharomyces cerevisiae | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Bradyrhizobium japonicum | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Pseudomonas fluorescens | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Canis lupus familiaris | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Mycobacterium tuberculosis | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Bacillus licheniformis | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Bacillus amyloliquefaciens | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | [Bacillus] caldolyticus | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Methanocaldococcus jannaschii | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Phormidium laminosum | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Rana sp. | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Caenorhabditis elegans | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Homo sapiens | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Rhodobacter capsulatus | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Schizosaccharomyces pombe | - |
mature proteins | - |
? | |
signal peptides from preproteins + H2O | Escherichia coli | 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 | mature proteins | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus amyloliquefaciens | - |
- |
- |
Bacillus licheniformis | - |
- |
- |
Bacillus subtilis | - |
- |
- |
Bradyrhizobium japonicum | - |
- |
- |
Caenorhabditis elegans | P34525 | - |
- |
Canis lupus familiaris | - |
dog | - |
Escherichia coli | - |
- |
- |
Gallus gallus | - |
chicken, hen | - |
Haemophilus influenzae | - |
- |
- |
Homo sapiens | Q15005 | human | - |
Methanocaldococcus jannaschii | - |
putative signal peptidase | - |
Mycobacterium tuberculosis | - |
- |
- |
no activity in Mycoplasma genitalium | - |
smallest genome of all known self-replicating organisms, lacks a gene with any recognizable similarity to the type I peptidase family | - |
Phormidium laminosum | - |
- |
- |
Pseudomonas fluorescens | - |
- |
- |
Rana sp. | - |
frog | - |
Rattus norvegicus | - |
rat | - |
Rhodobacter capsulatus | Q52697 | - |
- |
Saccharomyces cerevisiae | - |
yeast | - |
Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
Schizosaccharomyces pombe | Q10259 | - |
- |
Staphylococcus aureus | - |
- |
- |
[Bacillus] caldolyticus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | all known eukaryotic signal peptidase complexes contain a glycoprotein subunit | Gallus gallus |
glycoprotein | all known eukaryotic signal peptidase complexes contain a glycoprotein subunit | Saccharomyces cerevisiae |
glycoprotein | all known eukaryotic signal peptidase complexes contain a glycoprotein subunit | Rana sp. |
glycoprotein | all known eukaryotic signal peptidase complexes contain a glycoprotein subunit | Caenorhabditis elegans |
Purification (Comment) | Organism |
---|---|
- |
Gallus gallus |
- |
Escherichia coli |
- |
Canis lupus familiaris |
partially | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | Saccharomyces cerevisiae | ? | - |
? | |
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 | Escherichia coli | ? | - |
? | |
pro-ompA-nuclease + H2O | - |
Staphylococcus aureus | ompA-nuclease + ? | - |
? | |
pro-ompA-nuclease + H2O | - |
Bacillus subtilis | ompA-nuclease + ? | - |
? | |
pro-ompA-nuclease + H2O | - |
Bacillus amyloliquefaciens | ompA-nuclease + ? | - |
? | |
pro-ompA-nuclease + H2O | excellent substrate for microsomal signal peptidase | Gallus gallus | ompA-nuclease + ? | - |
? | |
pro-ompA-nuclease + H2O | 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 | Escherichia coli | ompA-nuclease + ? | - |
? | |
signal peptides from preproteins + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Gallus gallus | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Staphylococcus aureus | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Haemophilus influenzae | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Bacillus subtilis | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Rattus norvegicus | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Saccharomyces cerevisiae | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Bradyrhizobium japonicum | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Pseudomonas fluorescens | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Canis lupus familiaris | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Mycobacterium tuberculosis | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Bacillus licheniformis | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Bacillus amyloliquefaciens | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
[Bacillus] caldolyticus | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Methanocaldococcus jannaschii | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Phormidium laminosum | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Rana sp. | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Caenorhabditis elegans | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Homo sapiens | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Rhodobacter capsulatus | mature proteins | - |
? | |
signal peptides from preproteins + H2O | - |
Schizosaccharomyces pombe | mature proteins | - |
? | |
signal peptides from preproteins + H2O | 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 | Escherichia coli | mature proteins | - |
? | |
signal peptides from preproteins + H2O | 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 | Escherichia coli | mature proteins | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 1 * 23000 + 1 * 19000, gp23 and p19 | Gallus gallus |
pentamer | 1 * 25000 + 1 * 22000-23000 + 21000 + 18000 + 12000, subunits are named SP25, SP22/23, SPC21, SPC18, and SPC12, SDS-PAGE | Canis lupus familiaris |
tetramer | - |
Escherichia coli |
tetramer | 1 * 13000 + 1 * 18000 + 1 * 20000 + 1 * 25000 | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
canine signal peptidase complex | - |
Canis lupus familiaris |
imp1p | - |
Saccharomyces cerevisiae |
SipS | - |
Canis lupus familiaris |
SipU | - |
Canis lupus familiaris |
SPC | - |
Canis lupus familiaris |
SpsB | - |
Staphylococcus aureus |
type I signal peptidase | - |
Rattus norvegicus |
type I signal peptidase | - |
Saccharomyces cerevisiae |
type I signal peptidase | - |
Bradyrhizobium japonicum |
type I signal peptidase | - |
Pseudomonas fluorescens |
type I signal peptidase | - |
Canis lupus familiaris |
type I signal peptidase | - |
Mycobacterium tuberculosis |
type I signal peptidase | - |
Methanocaldococcus jannaschii |
type I signal peptidase | - |
Phormidium laminosum |
type I signal peptidase | - |
Rana sp. |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.04 | 1.97 | pro-ompA-nuclease | pH 8.0, 37°C | Escherichia coli | |
8.73 | - |
pro-ompA-nuclease | pH 8.0, 37°C | Escherichia coli |