Summary for peptidase A26.001: omptin

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Inhibitors

 

Names
MEROPS Nameomptin
Other namesOmpT g.p. (Escherichia coli), protease VII (Escherichia coli), protease 7 (Citrobacter rodentium), protease A
Domain architecture
MEROPS Classification
Classification Clan AF >> Subclan (none) >> Family A26 >> Subfamily (none) >> A26.001
Holotypeomptin (Escherichia coli), Uniprot accession P09169 (peptidase unit: 21-317), MERNUM MER0000606
History Identifier created: MEROPS 5.7 (17 December 2001)
Activity
Catalytic typeAspartic
PeplistIncluded in the Peplist with identifier PL00044
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.23 (Aspartic endopeptidases) >> Peptidase 3.4.23.49
EnzymologyBRENDA database
Proteolytic eventsCutDB database (16 cleavages)
BiotechnologyAn engineered variant of omptin has been proposed as a specific endopeptidase for the cleavage of recombinant fusion proteins (Okuno et al., 2004).
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/a/RKScissile bondRkq/a/a/g (based on 54 cleavages)
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Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 4 5 7 0 0 8 6 17
Pro 1 1 0 0 0 0 1 3
Ala 3 7 14 0 0 12 12 6
Val 1 2 0 0 2 7 3 0
Leu 9 6 4 0 0 5 2 0
Ile 2 1 2 0 0 5 0 2
Met 2 0 0 0 1 0 1 2
Phe 1 2 1 0 0 0 1 0
Tyr 0 2 5 0 0 1 0 0
Trp 4 2 0 0 0 0 3 0
Ser 0 2 2 1 1 2 1 1
Thr 1 2 3 0 0 1 1 2
Cys 1 0 0 0 0 0 0 0
Asn 0 0 2 0 0 1 0 0
Gln 1 1 4 0 7 0 4 2
Asp 4 1 0 0 0 0 0 4
Glu 5 0 5 0 0 1 4 4
Lys 2 5 0 16 13 4 1 2
Arg 5 8 1 37 30 3 7 3
His 1 0 0 0 0 0 0 1