Substrates for peptidase S06.002: EspP peptidase (Escherichia coli)

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates

Peptide and protein substrates that are thought to be physiologically relevant are indicated by P. Peptide and protein substrates that are thought to be pathologically relevant are indicated by D. Peptide and protein substrates that are not physiologically relevant are indicated by N. Synthetic substrates are indicated by S. Click on the symbol to show only physiological, non-physiological or synthetic substrates, or here to display all substrates. How cleavage sites have been identified are indicated by the following evidence codes: NT = N-terminal sequencing, MS = mass spectroscopy, MU = mutation, CS = consensus sequence, LC = liquid chromatography. To see all annotated cleavages for a protein substrate, click on the UniProt Accession.

Substrate Uniprot Residue range Cleavage Site Cleavage type Evidence P4 P3 P2 P1 P1' P2' P3' P4' Reference CutDB MERNUM
Ala-Ala-Pro-Leu-NHPhNO2 Ala-Ala-Pro-Leu+NHPhNO2 S Ala Ala Pro Leu NAN - - - Brookmeyer et al., 2007
eHEC-hlyA protein Q47461 1-998 peptide-Leu235+Ser-peptide P NT Ser Gly Ile Leu Ser Ala Val Ser Brockmeyer et al., 2011
espP peptidase Q7BSW5 1-1300 peptide-Asn1023+Asn-peptide P Asn Glu Val Asn Asn Leu Asn Lys Dautin et al., 2007 21068
pepsin A precursor P00791 16-385 peptide-Leu226+Gly-peptide N Val Val Leu Leu Gly Gly Ile Asp Brunder et al., 1997