Any feedback?
Literature summary for 3.4.21.89 extracted from
- The chemistry and enzymology of the type I signal peptidases (1997), Protein Sci., 6, 1129-1138.
Application
| 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(Commentary)
| 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 (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Inhibitors
| 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 [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0165 | - |
pro-ompA-nuclease | pH 8.0 | Escherichia coli |
Localization
| 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 [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/ Products (Substrates)
| 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
| 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
| 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 (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Gallus gallus |
- |
Escherichia coli |
- |
Canis lupus familiaris |
| partially | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| 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
| 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
| 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 [1/s]
| 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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
