CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.10 | Ribbon |
|
2.10.109 | Umud Fragment, subunit A |
|
2.10.109.10 | Umud Fragment, subunit A |
Domain Context
CATH Clusters
| Superfamily | Umud Fragment, subunit A |
| Functional Family | Signal peptidase I |
Enzyme Information
| 3.4.21.89 |
Signal peptidase I.
based on mapping to UniProt P00803
Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
-!- Unaffected by inhibitors of most serine peptidases, but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity. -!- Cleaves a single bond -Ala-|-Ala- in M13 phage procoat protein, producing free signal peptide and coat protein. -!- Eukaryote signal peptidases that may have somewhat different specificity are known from the endoplasmic reticulum membrane and mitochondrial inner membrane. -!- Belongs to peptidase family S26. -!- Formerly EC 3.4.99.36.
|
UniProtKB Entries (1)
| P00803 |
LEP_ECOLI
Escherichia coli K-12
Signal peptidase I
|
PDB Structure
| PDB | 1KN9 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism
J.Biol.Chem.
|
