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Structure of signal peptide peptidase A with C-termini bound in the active sites: insights into specificity, self-processing and regulation

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
E0006508biological_processproteolysis
E0008233molecular_functionpeptidase activity
F0006508biological_processproteolysis
F0008233molecular_functionpeptidase activity
G0006508biological_processproteolysis
G0008233molecular_functionpeptidase activity
H0006508biological_processproteolysis
H0008233molecular_functionpeptidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"22472423","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"22472423","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Cleavage; by autolysis"}
ChainResidueDetails

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PDB entries from 2025-10-15

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