3.4.23.49: omptin
This is an abbreviated version!
For detailed information about omptin, go to the full flat file.
Word Map on EC 3.4.23.49
-
3.4.23.49
-
furin
-
usp7
-
ubiquitin-specific
-
endoproteolytic
-
convertase
-
proproteins
-
deubiquitinating
-
prohormone
-
subtilisin-like
-
dibasic
-
yersinia
-
pestis
-
deubiquitinase
-
trans-golgi
-
propeptide
-
farnesylated
-
subtilisins
-
plague
-
kex2-like
-
lys-arg
-
proinsulins
-
prelamin
-
proregions
-
furin-like
-
flexneri
-
monobasic
-
deubiquitylation
-
exoprotease
-
zmpste24
-
isoprenylated
-
arg-arg
-
pharmacology
-
food industry
-
biotechnology
-
medicine
- 3.4.23.49
- furin
- usp7
-
ubiquitin-specific
-
endoproteolytic
-
convertase
- proproteins
-
deubiquitinating
-
prohormone
-
subtilisin-like
-
dibasic
- yersinia
- pestis
-
deubiquitinase
-
trans-golgi
- propeptide
-
farnesylated
- subtilisins
- plague
-
kex2-like
- lys-arg
- proinsulins
-
prelamin
-
proregions
-
furin-like
- flexneri
-
monobasic
-
deubiquitylation
-
exoprotease
- zmpste24
-
isoprenylated
- arg-arg
- pharmacology
- food industry
- biotechnology
- medicine
Reaction
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. =
Synonyms
bacterial outer-membrane protease, Citrobacter rodentium outer-membrane protease, CroP, E. coli protease VII, EC 3.4.21.87, endoprotease, Gene ompT proteins, More, OmpP, OmpP protease, ompT, OmpT protease, OmpT protein, Omptin, omptin protease, outer membrane protease, Outer membrane protein 3B, outer-membrane protease, outer-membrane protease T, PgtE, Pla, plaA, protease 7, Protease A, Protease VII, Protein a, Proteins, specific or class, gene ompT, SopA
ECTree
Advanced search results
General Information
General Information on EC 3.4.23.49 - omptin
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
metabolism
physiological function
additional information
comparative analysis of the sequences of the pro-omptin Pla (EC 3.4.23.48) with other omptin family proteases, such as PgtE from Salmonella enterica, SopA from Shigella flexneri, and OmpT and OmpP from Escherichia coli reveals the location of predicted linear B-cell epitopes in either identical positions or in a very close proximity to all nine Pla epitopes predicted from library, and identified serologically using human anti-Pla antisera, overview
evolution
comparative analysis of the sequences of the pro-omptin Pla (EC 3.4.23.48) with other omptin family proteases, such as PgtE from Salmonella enterica, SopA from Shigella flexneri, and OmpT and OmpP from Escherichia coli reveals the location of predicted linear B-cell epitopes in either identical positions or in a very close proximity to all nine Pla epitopes predicted from library, and identified serologically using human anti-Pla antisera, overview
evolution
the difference in CroP and OmpT substrate specificity suggests that omptins evolved in response to the substrates present in their host microenvironments
evolution
-
the difference in CroP and OmpT substrate specificity suggests that omptins evolved in response to the substrates present in their host microenvironments
evolution
the enzyme belongs to the omptin family of enzymes
evolution
Citrobacter rodentium ATCC 51459
-
the difference in CroP and OmpT substrate specificity suggests that omptins evolved in response to the substrates present in their host microenvironments
-
evolution
-
comparative analysis of the sequences of the pro-omptin Pla (EC 3.4.23.48) with other omptin family proteases, such as PgtE from Salmonella enterica, SopA from Shigella flexneri, and OmpT and OmpP from Escherichia coli reveals the location of predicted linear B-cell epitopes in either identical positions or in a very close proximity to all nine Pla epitopes predicted from library, and identified serologically using human anti-Pla antisera, overview
-
evolution
-
comparative analysis of the sequences of the pro-omptin Pla (EC 3.4.23.48) with other omptin family proteases, such as PgtE from Salmonella enterica, SopA from Shigella flexneri, and OmpT and OmpP from Escherichia coli reveals the location of predicted linear B-cell epitopes in either identical positions or in a very close proximity to all nine Pla epitopes predicted from library, and identified serologically using human anti-Pla antisera, overview
-
evolution
Citrobacter rodentium DBS 100
-
the difference in CroP and OmpT substrate specificity suggests that omptins evolved in response to the substrates present in their host microenvironments
-
evolution
Escherichia coli EDL933
-
the difference in CroP and OmpT substrate specificity suggests that omptins evolved in response to the substrates present in their host microenvironments
-
deletion of croP in Citrobacter rodentium results in higher susceptibility to alpha-helical antimicrobial peptides, indicating a direct role of CroP in antimicrobial peptide resistance. Transcriptional activation of PhoP-regulated genes by alpha-helical antimicrobial peptides is restored in the croP mutant
malfunction
-
Escherichia coli BL21(DE3) strain, which does not possess the ompT gene, no proteolysis of ZF-RNase-3 is observed
malfunction
-
using gene deletions, it is demonstrated that bacterial inactivation of tissue factor pathway inhibitor (TFPI) requires omptin expression
malfunction
-
using gene deletions, it is demonstrated that bacterial inactivation of tissue factor pathway inhibitor (TFPI) requires omptin expression
malfunction
-
human neutrophils interact less with serum-opsonized FITC-stained Salmonella enterica strain 14028R than with the isogenic DELTApgtE strain 14028R-1
malfunction
-
human neutrophils interact less with serum-opsonized FITC-stained Salmonella enterica strain 14028R than with the isogenic DELTApgtE strain 14028R-1
-
malfunction
-
Escherichia coli BL21(DE3) strain, which does not possess the ompT gene, no proteolysis of ZF-RNase-3 is observed
-
expression of PgtE is regulated by the SlyA regulator, which, on the other hand, is regulated by the PhoP/Q regulatory system which senses and responses to alpha-helical cationic antimicrobial peptides that are substrates for PgtE degradation
metabolism
-
the breakdown of factors B and H is critically dependent on the direct proteolytic activity exerted by omptins
metabolism
-
the breakdown of factors B and H is critically dependent on the direct proteolytic activity exerted by omptins
-
metabolism
-
expression of PgtE is regulated by the SlyA regulator, which, on the other hand, is regulated by the PhoP/Q regulatory system which senses and responses to alpha-helical cationic antimicrobial peptides that are substrates for PgtE degradation
-
metabolism
-
expression of PgtE is regulated by the SlyA regulator, which, on the other hand, is regulated by the PhoP/Q regulatory system which senses and responses to alpha-helical cationic antimicrobial peptides that are substrates for PgtE degradation
-
CroP greatly contributes to the protection of the outer membrane from antimicrobial peptides damage by actively degrading alpha-helical antimicrobial peptides before they reach the periplasmic space. Resistance to alpha-helical antimicrobial peptides by the extracellular pathogen Citrobacter rodentium relies primarily on the CroP outer membrane protease
physiological function
-
polymer exclusion experiments are used to probe the pore dimensions of the Vibrio cholerae OmpU and OmpT porins. The results show the lack of strict correlation between the conductance and pore size measured by polymer exclusion, as OmpT has a lower molecular weight cut off than OmpU, although its conductance is larger
physiological function
-
deletion mutant is more susceptible to alpha-helical antimicrobial peptides
physiological function
-
ompT deletion mutants are more susceptible to low molecular weight cationic peptides purified from human urine than wild-type strains. OmpT may help Escherichia coli persist longer in the urinary tract by enabling it to resist the antimicrobial activity of urinary cationic peptides
physiological function
-
OmpT is involved in the antimicrobial properties of Arg- and Lys-rich histones and the modes of antimicrobial action of these histones are different
physiological function
-
Citrobacter rodentium inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs)
physiological function
Escherichia coli OmpT inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively
physiological function
PgtE of the enteropathogen Salmonella enterica is a surface-exposed, transmembrane beta-barrel proteases of the omptin family that exhibit a complex array of interactions with the hemostatic systems in vitro, the protease is an established virulence factor. PgtE proteolysis targets control aspects of fibrinolysis, and mimicry of matrix metalloproteinases enhances cell migration that should favor the intracellular spread of the bacterium. The enzymatic activity of the protease is strongly influenced by the environment-induced variations in lipopolysaccharide that binds to the beta-barrel. The protease cleaves the tissue factor pathway inhibitor and thus also expresses procoagulant activity. PgtE effectively suppresses the regulatory proteins PAI-1, alpha2AP, and TAFI and activates scu-PA to active urokinase. PgtE addresses the control systems rather than direct plasminogen activation. Another mechanism by which PgtE can enhance cell motility and bacteria-phagocyte encounters is its ability to degrade gelatine and to activate the matrix metalloproteinase 9 (procollagenase) secreted from macrophages. PgtE also enhances multiplication of Salmonella enterica inside murine macrophages, where degradation of cationic antimicrobial peptides seems an important function of PgtE. PgtE also inactivates the complement regulatory proteins factors B and H and reduces opsonophacytosis of Salmonella enterica
physiological function
-
the virulence factor PgtE is an outer membrane protease (omptin) of the zoonotic pathogen Salmonella enterica. PgtE of Salmonella enterica interferes with the alternative complement pathway by cleaving factors B and H. In human serum, C3 cleavage is dependent on proteolytically active PgtE. PgtE inhibits opsonization of Slamonella enterica strain 14028R. Cleavage of H abolishes its complement regulatory activity leading to increased formation of C3b, whereas cleavage of B leads to fewer active C3 convertases and decreased formation of C3b. PgtE competes with B and H for C3/C3b cleavage, because B fragment Bb in the C3-convertase cleaves C3, and H is a cofactor for C3b cleavage by factor I
physiological function
Citrobacter rodentium ATCC 51459
-
Citrobacter rodentium inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs)
-
physiological function
-
the virulence factor PgtE is an outer membrane protease (omptin) of the zoonotic pathogen Salmonella enterica. PgtE of Salmonella enterica interferes with the alternative complement pathway by cleaving factors B and H. In human serum, C3 cleavage is dependent on proteolytically active PgtE. PgtE inhibits opsonization of Slamonella enterica strain 14028R. Cleavage of H abolishes its complement regulatory activity leading to increased formation of C3b, whereas cleavage of B leads to fewer active C3 convertases and decreased formation of C3b. PgtE competes with B and H for C3/C3b cleavage, because B fragment Bb in the C3-convertase cleaves C3, and H is a cofactor for C3b cleavage by factor I
-
physiological function
-
PgtE of the enteropathogen Salmonella enterica is a surface-exposed, transmembrane beta-barrel proteases of the omptin family that exhibit a complex array of interactions with the hemostatic systems in vitro, the protease is an established virulence factor. PgtE proteolysis targets control aspects of fibrinolysis, and mimicry of matrix metalloproteinases enhances cell migration that should favor the intracellular spread of the bacterium. The enzymatic activity of the protease is strongly influenced by the environment-induced variations in lipopolysaccharide that binds to the beta-barrel. The protease cleaves the tissue factor pathway inhibitor and thus also expresses procoagulant activity. PgtE effectively suppresses the regulatory proteins PAI-1, alpha2AP, and TAFI and activates scu-PA to active urokinase. PgtE addresses the control systems rather than direct plasminogen activation. Another mechanism by which PgtE can enhance cell motility and bacteria-phagocyte encounters is its ability to degrade gelatine and to activate the matrix metalloproteinase 9 (procollagenase) secreted from macrophages. PgtE also enhances multiplication of Salmonella enterica inside murine macrophages, where degradation of cationic antimicrobial peptides seems an important function of PgtE. PgtE also inactivates the complement regulatory proteins factors B and H and reduces opsonophacytosis of Salmonella enterica
-
physiological function
-
ompT deletion mutants are more susceptible to low molecular weight cationic peptides purified from human urine than wild-type strains. OmpT may help Escherichia coli persist longer in the urinary tract by enabling it to resist the antimicrobial activity of urinary cationic peptides
-
physiological function
-
PgtE of the enteropathogen Salmonella enterica is a surface-exposed, transmembrane beta-barrel proteases of the omptin family that exhibit a complex array of interactions with the hemostatic systems in vitro, the protease is an established virulence factor. PgtE proteolysis targets control aspects of fibrinolysis, and mimicry of matrix metalloproteinases enhances cell migration that should favor the intracellular spread of the bacterium. The enzymatic activity of the protease is strongly influenced by the environment-induced variations in lipopolysaccharide that binds to the beta-barrel. The protease cleaves the tissue factor pathway inhibitor and thus also expresses procoagulant activity. PgtE effectively suppresses the regulatory proteins PAI-1, alpha2AP, and TAFI and activates scu-PA to active urokinase. PgtE addresses the control systems rather than direct plasminogen activation. Another mechanism by which PgtE can enhance cell motility and bacteria-phagocyte encounters is its ability to degrade gelatine and to activate the matrix metalloproteinase 9 (procollagenase) secreted from macrophages. PgtE also enhances multiplication of Salmonella enterica inside murine macrophages, where degradation of cationic antimicrobial peptides seems an important function of PgtE. PgtE also inactivates the complement regulatory proteins factors B and H and reduces opsonophacytosis of Salmonella enterica
-
physiological function
-
OmpT is involved in the antimicrobial properties of Arg- and Lys-rich histones and the modes of antimicrobial action of these histones are different
-
physiological function
Citrobacter rodentium DBS 100
-
Citrobacter rodentium inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs)
-
physiological function
-
deletion mutant is more susceptible to alpha-helical antimicrobial peptides
-
physiological function
Escherichia coli EDL933
-
Escherichia coli OmpT inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively
-
physiological function
Escherichia coli EPEC / E2348/69
-
deletion mutant is more susceptible to alpha-helical antimicrobial peptides
-
acidic residues in the active site are the catalytic pairs Asp83-Asp85 and His212-Asp210
additional information
PgtE three-dimensional structure homology modelling using structure with PDB ID 1I78 as a template. Residues Glu29, Leu30, His 208, Phe 215, Glu 217 and Ala 275 occupy the active site