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Literature summary for 3.4.23.49 extracted from

  • Kukkonen, M.; Korhonen, T.K.
    The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis (2004), Int. J. Med. Microbiol., 294, 7-14.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
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
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
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
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
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

Cloned(Commentary)

Cloned (Comment) Organism
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
gene pla is 9.5 kb plasmid pPCP1 encoded, phylogenetic tree of the omptin family Yersinia pestis
the gene pgtE is encoded on the chromosome, phylogenetic tree of the omptin family Salmonella enterica
the gene plaA is 36 kb plasmid pEP36 encoded, phylogenetic tree of the omptin family Erwinia pyrifoliae
the gene sopA is 210 kb virulence plasmid pWR100-encoded, phylogenetic tree of the omptin family Shigella flexneri

Crystallization (Commentary)

Crystallization (Comment) Organism
structure analysis Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
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
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
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
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
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

Localization

Localization Comment Organism GeneOntology No. Textmining
outer membrane
-
Escherichia coli 19867
-
outer membrane
-
Yersinia pestis 19867
-
outer membrane
-
Salmonella enterica 19867
-
outer membrane
-
Shigella flexneri 19867
-
outer membrane
-
Erwinia pyrifoliae 19867
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cationic antimicrobial peptides from epithelial cells or macrophages + H2O Salmonella enterica
-
?
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O Escherichia coli OmpT, proteolytic degradation ?
-
?
human antiprotease alpha2-antiplasmin + H2O Yersinia pestis involved in infection and pathogenesis ?
-
?
human circulating complement proteins + H2O Yersinia pestis activation of the substrate ?
-
?
human proenzyme plasminogen + H2O Salmonella enterica activation of the substrate by proteolytic cleavage ?
-
?
human proenzyme plasminogen + H2O Yersinia pestis involved in pathogenic tissue invasion or nutrition ?
-
?
human proenzyme plasminogen + H2O Escherichia coli low activity of OmpT in activation of the substrate, proteolytic cleavage ?
-
?
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 ?
-
?
additional information Salmonella enterica the enzyme is important in the intracellular phases of salmonellosis, the multifunctional enzyme has virulence-associated functions ?
-
?
additional information Shigella flexneri the enzyme is important in the intracellular phases of shigellosis, the multifunctional enzyme has virulence-associated functions ?
-
?
additional information Escherichia coli the multifunctional enzyme has a virulence-associated function in protein degradation ?
-
?
additional information Erwinia pyrifoliae the multifunctional enzyme has virulence-associated functions ?
-
?
small-molecular-weight chromogenic peptides + H2O Escherichia coli OmpT, proteolytic cleavage ?
-
?

Organism

Organism UniProt Comment Textmining
Erwinia pyrifoliae
-
-
-
Escherichia coli
-
-
-
Salmonella enterica
-
-
-
Shigella flexneri
-
-
-
Yersinia pestis
-
human pathogen
-

Reaction

Reaction Comment Organism Reaction ID
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
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
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
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
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
-
Salmonella enterica ?
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O OmpT, proteolytic degradation Escherichia coli ?
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O proteolytic degradation Salmonella enterica ?
-
?
human antiprotease alpha2-antiplasmin + H2O involved in infection and pathogenesis Yersinia pestis ?
-
?
human antiprotease alpha2-antiplasmin + H2O inactivation of the substrate by proteolytic cleavage Yersinia pestis ?
-
?
human circulating complement proteins + H2O activation of the substrate Yersinia pestis ?
-
?
human circulating complement proteins + H2O activation of the substrate by proteolytic cleavage Yersinia pestis ?
-
?
human proenzyme plasminogen + H2O activation of the substrate by proteolytic cleavage Yersinia pestis ?
-
?
human proenzyme plasminogen + H2O activation of the substrate by proteolytic cleavage Salmonella enterica ?
-
?
human proenzyme plasminogen + H2O involved in pathogenic tissue invasion or nutrition Yersinia pestis ?
-
?
human proenzyme plasminogen + H2O low activity of OmpT in activation of the substrate, proteolytic cleavage Escherichia coli ?
-
?
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 ?
-
?
additional information the enzyme is important in the intracellular phases of salmonellosis, the multifunctional enzyme has virulence-associated functions Salmonella enterica ?
-
?
additional information the enzyme is important in the intracellular phases of shigellosis, the multifunctional enzyme has virulence-associated functions Shigella flexneri ?
-
?
additional information the multifunctional enzyme has a virulence-associated function in protein degradation Escherichia coli ?
-
?
additional information the multifunctional enzyme has virulence-associated functions Erwinia pyrifoliae ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
small-molecular-weight chromogenic peptides + H2O OmpT, proteolytic cleavage Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
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

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins Yersinia pestis
More the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins Salmonella enterica
More the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins Shigella flexneri
More the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins Erwinia pyrifoliae
More the enzymes belong to the omptin family of enterobacterial surface proteases/adhesins Escherichia coli
OmpP
-
Escherichia coli
ompT
-
Escherichia coli
PgtE
-
Salmonella enterica
plaA
-
Erwinia pyrifoliae
SopA
-
Shigella flexneri