Family U69


Summary Holotypes Alignment Tree Genomes Structure Literature

Summary for family U69

Family type peptidaseU69.001 - AIDA-I self-cleaving autotransporter protein (Escherichia coli) (Escherichia coli), MEROPS Accession MER0152704 (peptidase unit: 847-904)
Content of familyFamily U69 contains self-processing peptidases.
History Identifier created: MEROPS 8.5 (24 August 2009)
The adhesin AIDA-I is a plasmid-encoded protein from Escherichia coli which plays a role in infantile diarrhaea in pigs. AIDA-I is a monomeric autotransporter secreted by the type Va secretory pathway and the extracellular portion is autocatalytically released.
Catalytic typePeptidase of unknown catalytic type
Active siteAlthough the active site residues responsible for the autoprocessing have not been unequivocally identified, site-directed mutagenesis of Asp878 or Glu897 prevented cleavage (Charbonneau et al., 2009).
Activities and specificitiesSelf-processing occurs at the Ser846Ala bond.
Molecular structureAIDA-I is synthesized as a preproprotein with an N-terminal signal peptide promoting secretion into the periplasm. A C-terminal membrane-embedded domain, known as the AIDA-I translocator, permits secretion of part of the protein across the outer membrane. The extracellular domain, which is the adhesin, then releases itself, but remains associated with the translocator domain. The region of the protein responsible for cleavage lies between Ala667 and Thr953 (Charbonneau et al., 2009).
Distribution of family Bacteria details  
Archaea -  
Protozoa details  
Fungi details  
Plants details  
Animals details  
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Biological functions
Statistics for family U69Sequences:661
Identifiers with PDB entries:2
Downloadable files Sequence library (FastA format)
Sequence alignment (FastA format)
Phylogenetic tree (Newick format)
Peptidases and Homologues MEROPS ID Structure
AIDA-I self-cleaving autotransporter protein (Escherichia coli)U69.001Yes
YfaL protein (Escherichi coli)U69.A11-
family U69 unassigned peptidasesunassignedYes