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.
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UniProtKB Entries (1)
P00803 |
LEP_ECOLI
Escherichia coli K-12
Signal peptidase I
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PDB Structure
PDB | 3S04 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Synthesis and characterization of the arylomycin lipoglycopeptide antibiotics and the crystallographic analysis of their complex with signal peptidase.
J.Am.Chem.Soc.
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