EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.4.23.49 | lipopolysaccharide | i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain | Escherichia coli | |
3.4.23.49 | lipopolysaccharide | i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain | Yersinia pestis | |
3.4.23.49 | lipopolysaccharide | i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain | Salmonella enterica | |
3.4.23.49 | lipopolysaccharide | i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain | Shigella flexneri | |
3.4.23.49 | lipopolysaccharide | i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain | Erwinia pyrifoliae |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.23.49 | gene ompT is located on the chromosome and a cryptic prophage, gene ompP is 95 kb F-plasmid-encoded, phylogenetic tree of the omptin family | Escherichia coli |
3.4.23.49 | gene pla is 9.5 kb plasmid pPCP1 encoded, phylogenetic tree of the omptin family | Yersinia pestis |
3.4.23.49 | the gene pgtE is encoded on the chromosome, phylogenetic tree of the omptin family | Salmonella enterica |
3.4.23.49 | the gene plaA is 36 kb plasmid pEP36 encoded, phylogenetic tree of the omptin family | Erwinia pyrifoliae |
3.4.23.49 | the gene sopA is 210 kb virulence plasmid pWR100-encoded, phylogenetic tree of the omptin family | Shigella flexneri |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.4.23.49 | structure analysis | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.23.49 | lipopolysaccharide | i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain | Erwinia pyrifoliae | |
3.4.23.49 | lipopolysaccharide | i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain | Escherichia coli | |
3.4.23.49 | lipopolysaccharide | i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain | Salmonella enterica | |
3.4.23.49 | lipopolysaccharide | i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain | Shigella flexneri | |
3.4.23.49 | lipopolysaccharide | i.e. LPS, rough, dependent on, interacts with the beta-barrel in the outer membrane, function and mechanism overview, smooth LPS sterically inhibits the enzyme via its O-side chain | Yersinia pestis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.23.49 | outer membrane | - |
Escherichia coli | 19867 | - |
3.4.23.49 | outer membrane | - |
Yersinia pestis | 19867 | - |
3.4.23.49 | outer membrane | - |
Salmonella enterica | 19867 | - |
3.4.23.49 | outer membrane | - |
Shigella flexneri | 19867 | - |
3.4.23.49 | outer membrane | - |
Erwinia pyrifoliae | 19867 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.23.49 | cationic antimicrobial peptides from epithelial cells or macrophages + H2O | Salmonella enterica | - |
? | - |
? | |
3.4.23.49 | cationic antimicrobial peptides from epithelial cells or macrophages + H2O | Escherichia coli | OmpT, proteolytic degradation | ? | - |
? | |
3.4.23.49 | human antiprotease alpha2-antiplasmin + H2O | Yersinia pestis | involved in infection and pathogenesis | ? | - |
? | |
3.4.23.49 | human circulating complement proteins + H2O | Yersinia pestis | activation of the substrate | ? | - |
? | |
3.4.23.49 | human proenzyme plasminogen + H2O | Salmonella enterica | activation of the substrate by proteolytic cleavage | ? | - |
? | |
3.4.23.49 | human proenzyme plasminogen + H2O | Yersinia pestis | involved in pathogenic tissue invasion or nutrition | ? | - |
? | |
3.4.23.49 | human proenzyme plasminogen + H2O | Escherichia coli | low activity of OmpT in activation of the substrate, proteolytic cleavage | ? | - |
? | |
3.4.23.49 | additional information | Yersinia pestis | substrate specificity, the multifunctional enzyme has virulence-associated functions for invasion of human epithelial cells, its binding to laminin localizes the uncontrolled plasmin activity onto basement membranes, the enzyme is involved in spread of the bacterium through tissue barriers due to its adhesive function | ? | - |
? | |
3.4.23.49 | additional information | Salmonella enterica | the enzyme is important in the intracellular phases of salmonellosis, the multifunctional enzyme has virulence-associated functions | ? | - |
? | |
3.4.23.49 | additional information | Shigella flexneri | the enzyme is important in the intracellular phases of shigellosis, the multifunctional enzyme has virulence-associated functions | ? | - |
? | |
3.4.23.49 | additional information | Escherichia coli | the multifunctional enzyme has a virulence-associated function in protein degradation | ? | - |
? | |
3.4.23.49 | additional information | Erwinia pyrifoliae | the multifunctional enzyme has virulence-associated functions | ? | - |
? | |
3.4.23.49 | small-molecular-weight chromogenic peptides + H2O | Escherichia coli | OmpT, proteolytic cleavage | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.23.49 | Erwinia pyrifoliae | - |
- |
- |
3.4.23.49 | Escherichia coli | - |
- |
- |
3.4.23.49 | Salmonella enterica | - |
- |
- |
3.4.23.49 | Shigella flexneri | - |
- |
- |
3.4.23.49 | Yersinia pestis | - |
human pathogen | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.4.23.49 | Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. | the enzyme contains a Ser-Asp-His catalytic triad, active site, the consensus sequence of OmpT is R/K-R/K-A, the enzyme is highly selective for a basic amino acid residue at position P1, but less exclusive at P1', where several amino acids are tolerated, OmpP shows similar specificity, minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme | Escherichia coli | |
3.4.23.49 | Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. | the enzyme contains a Ser-Asp-His catalytic triad, active site, the enzyme prefers a basic amino acid residue at position P1, but is less exclusive at P1', where several amino acids are tolerated, minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme | Yersinia pestis | |
3.4.23.49 | Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. | the enzyme contains a Ser-Asp-His catalytic triad, active site, the enzyme prefers a basic amino acid residue at position P1, but is less exclusive at P1', where several amino acids are tolerated, minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme | Salmonella enterica | |
3.4.23.49 | Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. | the enzyme contains a Ser-Asp-His catalytic triad, active site, the enzyme prefers a basic amino acid residue at position P1, but is less exclusive at P1', where several amino acids are tolerated, minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme | Shigella flexneri | |
3.4.23.49 | Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. | the enzyme contains a Ser-Asp-His catalytic triad, active site, the enzyme prefers a basic amino acid residue at position P1, but is less exclusive at P1', where several amino acids are tolerated, minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme | Erwinia pyrifoliae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.23.49 | cationic antimicrobial peptides from epithelial cells or macrophages + H2O | - |
Salmonella enterica | ? | - |
? | |
3.4.23.49 | cationic antimicrobial peptides from epithelial cells or macrophages + H2O | OmpT, proteolytic degradation | Escherichia coli | ? | - |
? | |
3.4.23.49 | cationic antimicrobial peptides from epithelial cells or macrophages + H2O | proteolytic degradation | Salmonella enterica | ? | - |
? | |
3.4.23.49 | human antiprotease alpha2-antiplasmin + H2O | involved in infection and pathogenesis | Yersinia pestis | ? | - |
? | |
3.4.23.49 | human antiprotease alpha2-antiplasmin + H2O | inactivation of the substrate by proteolytic cleavage | Yersinia pestis | ? | - |
? | |
3.4.23.49 | human circulating complement proteins + H2O | activation of the substrate | Yersinia pestis | ? | - |
? | |
3.4.23.49 | human circulating complement proteins + H2O | activation of the substrate by proteolytic cleavage | Yersinia pestis | ? | - |
? | |
3.4.23.49 | human proenzyme plasminogen + H2O | activation of the substrate by proteolytic cleavage | Yersinia pestis | ? | - |
? | |
3.4.23.49 | human proenzyme plasminogen + H2O | activation of the substrate by proteolytic cleavage | Salmonella enterica | ? | - |
? | |
3.4.23.49 | human proenzyme plasminogen + H2O | involved in pathogenic tissue invasion or nutrition | Yersinia pestis | ? | - |
? | |
3.4.23.49 | human proenzyme plasminogen + H2O | low activity of OmpT in activation of the substrate, proteolytic cleavage | Escherichia coli | ? | - |
? | |
3.4.23.49 | additional information | substrate specificity, the multifunctional enzyme has virulence-associated functions for invasion of human epithelial cells, its binding to laminin localizes the uncontrolled plasmin activity onto basement membranes, the enzyme is involved in spread of the bacterium through tissue barriers due to its adhesive function | Yersinia pestis | ? | - |
? | |
3.4.23.49 | additional information | the enzyme is important in the intracellular phases of salmonellosis, the multifunctional enzyme has virulence-associated functions | Salmonella enterica | ? | - |
? | |
3.4.23.49 | additional information | the enzyme is important in the intracellular phases of shigellosis, the multifunctional enzyme has virulence-associated functions | Shigella flexneri | ? | - |
? | |
3.4.23.49 | additional information | the multifunctional enzyme has a virulence-associated function in protein degradation | Escherichia coli | ? | - |
? | |
3.4.23.49 | additional information | the multifunctional enzyme has virulence-associated functions | Erwinia pyrifoliae | ? | - |
? | |
3.4.23.49 | additional information | minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme | Salmonella enterica | ? | - |
? | |
3.4.23.49 | additional information | minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme | Shigella flexneri | ? | - |
? | |
3.4.23.49 | additional information | minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme | Erwinia pyrifoliae | ? | - |
? | |
3.4.23.49 | additional information | no proteolytic cleavage of laminin or of small-molecular-weight chromogenic peptides, minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme | Yersinia pestis | ? | - |
? | |
3.4.23.49 | additional information | substrate specificity, OmpT shows no activity with antiprotease alpha2-antiplasmin, minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme | Escherichia coli | ? | - |
? | |
3.4.23.49 | small-molecular-weight chromogenic peptides + H2O | OmpT, proteolytic cleavage | Escherichia coli | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.23.49 | More | OmpT possesses a beta-barrel fold with 10 antiparallel beta-strands connected by 4 short periplasmic turns and 5 extracellular loops in the outer membrane | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.23.49 | More | the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins | Yersinia pestis |
3.4.23.49 | More | the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins | Salmonella enterica |
3.4.23.49 | More | the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins | Shigella flexneri |
3.4.23.49 | More | the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins | Erwinia pyrifoliae |
3.4.23.49 | More | the enzymes belong to the omptin family of enterobacterial surface proteases/adhesins | Escherichia coli |
3.4.23.49 | OmpP | - |
Escherichia coli |
3.4.23.49 | ompT | - |
Escherichia coli |
3.4.23.49 | PgtE | - |
Salmonella enterica |
3.4.23.49 | plaA | - |
Erwinia pyrifoliae |
3.4.23.49 | SopA | - |
Shigella flexneri |