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Literature summary extracted from

  • Vandeputte-Rutten, L.; Kramer, R.A.; Kroon, J.; Dekker, N.; Egmond, M.R.; Gros, P.
    Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site (2001), EMBO J., 20, 5033-5039.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.23.49 lipopolysaccharide displays enzymatic activity in vitro only in presence Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.23.49 overexpressed without its signal sequence in Escherichia coli K-12 strain DH5alpha using a T7 system Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.23.49 hanging drop vapour diffusion method, space group P3(2)21, unit cell parameters a : B : 98.39 A, c : 165.70 A Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.4.23.49 G216K/K217G recombinant ompT variant in order to abolish autoproteolysis Escherichia coli
3.4.23.49 S99A/G216K/K217G recombinant ompT variant in order to abolish autoproteolysis Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.23.49 membrane integral membrane protease, outer membrane, membrane bound Escherichia coli 16020
-

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.49 Escherichia coli
-
-
-

Synonyms

EC Number Synonyms Comment Organism
3.4.23.49 ompT
-
 Escherichia coli