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Literature summary for 3.4.21.89 extracted from
- Signal peptidase I processed secretory signal sequences selection for and against specific amino acids at the second position of mature protein (2017), Biochem. Biophys. Res. Commun., 483, 972-977 .
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cell membrane | - |
Methanococcus voltae | - |
- |
| cell membrane | - |
Sulfurisphaera tokodaii | - |
- |
| cell membrane | - |
Escherichia coli | - |
- |
| cell membrane | - |
Bacillus subtilis | - |
- |
| cell membrane | - |
Saccharomyces cerevisiae | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | P28628 | - |
- |
| Bacillus subtilis 168 | P28628 | - |
- |
| Escherichia coli | P00803 | - |
- |
| Methanococcus voltae | - |
- |
- |
| Methanococcus voltae A3 | - |
- |
- |
| Saccharomyces cerevisiae | P15367 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | P15367 | - |
- |
| Sulfurisphaera tokodaii | - |
- |
- |
| Sulfurisphaera tokodaii 7 | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | Escherichia coli | ? | - |
? |  |
| 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 | Bacillus subtilis | ? | - |
? | |
| 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 | Methanococcus voltae | ? | - |
? | |
| 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 | Sulfurisphaera tokodaii | ? | - |
? | |
| 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 | Saccharomyces cerevisiae | ? | - |
? | |
| 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 | Bacillus subtilis 168 | ? | - |
? | |
| 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 | Sulfurisphaera tokodaii 7 | ? | - |
? | |
| 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 | Methanococcus voltae A3 | ? | - |
? | |
| 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 | Saccharomyces cerevisiae ATCC 204508 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LepB | - |
Escherichia coli |
| SEC11 | - |
Saccharomyces cerevisiae |
| secretory protein 11 | - |
Saccharomyces cerevisiae |
| SipS | - |
Bacillus subtilis |
| SP I | - |
Methanococcus voltae |
| SP I | - |
Sulfurisphaera tokodaii |
| SP I | - |
Escherichia coli |
| SP I | - |
Bacillus subtilis |
| SP I | - |
Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Methanococcus voltae |
| 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 | Sulfurisphaera tokodaii |
| 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 | Saccharomyces cerevisiae |
| 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 | Bacillus subtilis |
| 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 | Escherichia coli |
| 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 | Methanococcus voltae |
| 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 | Sulfurisphaera tokodaii |
| 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 | Escherichia coli |
| 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 | Bacillus subtilis |
| 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 | Saccharomyces cerevisiae |
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