CATH Classification

Domain Context

CATH Clusters

Superfamily 2.170.230.10
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 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.
Liu, J., Luo, C., Smith, P.A., Chin, J.K., Page, M.G., Paetzel, M., Romesberg, F.E.
J.Am.Chem.Soc.
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