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Information on EC 3.4.23.49 - omptin
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3.4.23.49 omptinSpecify your search results
Word Map
- 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
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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
endoprotease, protease 7, outer membrane protease, omptin, ompt protease, protease vii, ompt protein, omptin protease, outer-membrane protease, outer-membrane protease t, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CroP
EC 3.4.21.87
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-
formerly
-
Gene ompT proteins
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-
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OmpP
OmpP protease
F episome-encoded outer membrane protease, 71% amino acid sequence identity with OmpT protease
ompT
OmpT protease
Omptin
-
-
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omptin protease
outer membrane protease
Outer membrane protein 3B
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-
-
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PgtE
Pla
-
-
-
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protease 7
Protease A
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-
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Protease VII
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Protein a
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Proteins, specific or class, gene ompT
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-
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additional information
ompT
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-
OmpT protease
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-
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additional information
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the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins
additional information
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the enzymes belong to the omptin family of enterobacterial surface proteases/adhesins
additional information
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the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins
additional information
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the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins
additional information
-
the enzyme belongs to the omptin family of enterobacterial surface proteases/adhesins
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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.
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.
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-
-
-
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.
active site structure, catalytic residues are Asp210 an His212, molecular dynamic simulations reveal substrate binding structure and structural requirements for the catalytic mechanism
-
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 consensus sequence of OmpT is R/K-A, the enzyme is highly selective for a basic amino acid residue at position P1, but less exclusive at P1', where several non-basic amino acids are tolerated, enzyme residue Asp97 is responsible for interaction with P1' position substrate residue
-
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, 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 e,g, Lys, Val, and Gly, at P2' common residues are Ala or Val, at P3 and P4 the enzyme prefers Trp or Arg
-
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
-
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
-
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
-
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
-
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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
150770-86-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-AKRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
-
-
-
?
2-aminobenzoyl-ARRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
2-aminobenzoyl-Ala-Arg + Arg-Ala-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
-
-
?
2-aminobenzoyl-IRRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
2-aminobenzoyl-Ile-Arg + Arg-Ala-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
2-aminobenzoyl-KLKSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLK + SSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
2-aminobenzoyl-KLRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLR + SSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
2-aminobenzoyl-KLRSSVQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLR + SSVQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
2-aminobenzoyl-KMRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KMR + SSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
2-aminobenzoyl-KNRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KNR + SSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
2-aminobenzoyl-KQRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KQR + SSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
-
-
-
?
2-aminobenzoyl-RRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
2-aminobenzoyl-L-Arg + Arg-Ala-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
a fusion-motilin peptide + H2O
?
-
proteolytic cleavage by mutant D97M at R-R-R-A-R*-motilin
-
-
?
Ac-GLLGDFARRAKEKIGC + H2O
Ac-GLLGDFAR + RAKEKIGC
LL37 substrate mutant
-
-
?
Ac-GLLGDFFRKSKEKIGC + H2O
Ac-GLLGDFF + RKSKEKIGC
LL37 substrate mutant, enzyme mutant G216K/K217G shows negligible activity
-
-
?
Ac-GLLGDFFRRVKEKIGC + H2O
Ac-GLLGDFFR + RVKEKIGC
LL37 substrate mutant
-
-
?
ALYKKLLKKLLKSAKKLG + H2O
?
synthetic alpha-antimicrobial peptide L-C18G, D-amino acids are not degraded by CroP
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-
?
aminobenzoyl-Ala-Arg-Arg-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
?
cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP, a murine cathelicidin-related antimicrobial peptide
-
-
?
ColE2-Im2 protein complex + H2O
?
-
a small amount of the endonuclease colicin E2 associated with the cognate immunity protein Im2, is susceptible to proteolytic cleavage by omptin. The presence of outer membrane protein BtuB is required for ColE-Im2 cleavage by omptin. The amount of colicin cleaved is greatly enhanced when ColE2 is dissociated from Im2. Omptin cleaves the C-terminal DNase domain of the toxin. Strains that over-produce OmpT are less susceptible to infection by ColE2 than by ColE2-Im2
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-
?
dynorphin A(1-13) + H2O
Tyr-Gly-Gly-Phe-Leu-Arg + Arg-Ile-Arg-Pro-Lys-Leu-Lys
-
proteolytic cleavage site GFLR*RIRPK
-
-
?
gamma-interferon + H2O
?
-
proteolytic cleavage sites KTGK*RKRSQ and FRGR*RASQ
-
-
?
gelatine + H2O
?
degradation
-
-
?
GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ + H2O
?
synthetic alpha-antimicrobial peptide CRAMP
-
-
?
H-NS + H2O
?
-
ompT cleaves preferentially at a C-terminal site, cleaves H-NS primarily between residues at positions 88-89 of the protein
-
?
human adrenocorticotropic hormone + H2O
?
-
proteolytic cleavage by mutant D97L at Ser24, release of the hormone
-
-
?
human calcitonin precursor + H2O
?
-
proteolytic cleavage by mutant D97H at an N-terminal Cys
-
-
?
human creatin kinase + H2O
?
-
proteolytic cleavage site DIYK*KLRDK
-
-
?
human plasminogen + H2O
?
-
proteolytic cleavage site CPGR*VVGGC, activation
-
-
?
L-Ala-L-Arg-L-Arg-L-Ala + H2O
L-Ala-L-Arg + L-Arg-L-Ala
-
model peptide substrate
-
-
?
N-acetyl-Ala-Arg-Arg-Ala-methylamide + H2O
?
fluctuations of outer-membrane protease OmpT in complex with its substrate Ala-Arg-Arg-Ala (ARRA) on microsecond timescale analyzed, effect of key point mutations at the active site studied
-
-
?
OmpT proteolytic site of the GFP + H2O
?
-
the construction of two GFP variants with modified putative OmpT proteolytic sites by site directed mutagenesis is described. Such modified genes upon arabinose induction exhibit varied degrees of GFP fluorescence. While the mutation of K79G/R80A close to the fluorophore results in dramatic loss of fluorescence activity, the modification of K214A/R215A results in four fold enhanced fluorescence of GFP K214A/R215
-
-
?
Parathyroid hormone + H2O
?
-
proteolytic cleavage sites EWLR*KKLQD and WLRK*KLQDV
-
-
?
Parathyroid hormone13-34 + H2O
?
-
human, cleaved at both Arg25-Lys26 and Lys26-Lys27
-
-
?
plasminogen + H2O
?
-
poor substrate
no formation of plasmin light chain
-
?
plasminogen + H2O
heavy and light chain of plasmin + ?
-
cleavage at an Arg-Val bond
-
?
plasminogen activator inhibitor-1 + H2O
?
inactivation
-
-
?
Protein expressed from a fusion gene + H2O
?
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the fusion gene is constructed by ligating the genetic information for the C-terminal 60 amino acids of E. coli hemolysin to the ces gene for a cholesterol esterase/lipase from a Pseudomonas species, OmpT protease preferentially recognizes potential cleavage sites within the linker sequence
-
-
?
rabbit creatine kinase + H2O
?
-
proteolytic cleavage sites DLYK*KLRDK and RGER*RAVEK
-
-
?
Recombinant human gamma-interferon + H2O
?
-
cleavage between basic amino acids
-
-
?
small-molecular-weight chromogenic peptides + H2O
?
-
OmpT, proteolytic cleavage
-
-
?
Tryptophan synthase + H2O
?
-
beta-subunit of E. coli enzyme, the wild-type beta-subunit is apparently very stable, the missense mutant beta(B8), carrying an amino acid switch from Gly to Arg at the residue 281, undergoes specific proteolytic cleavage, cleavage products of 30000 MW from the N-terminus and 13000 MW from the C-terminus are observed, cleavage is specific for the peptide bond Arg281-Met282
-
-
?
WCARVGKGRGR-NH2 + H2O
WCA + RVGKGRGR-NH2
-
proteolytic cleavage of the peptide at the site A-R
-
-
?
WEEGGRRIGRGGK + H2O
?
used as a control substrate for determination of the activity of OmpT protease
-
-
?
WEEGGRRIGRGGK-NH2 + H2O
WEEGGR + RIGRGGK-NH2
-
proteolytic cleavage of the peptide at the site R-R, no activity of mutant S223R, preferred substrate of wild-type OmpT
-
-
?
2-aminobenzoyl-AKKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
-
-
-
-
?
2-aminobenzoyl-AKKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
-
-
-
?
2-aminobenzoyl-ARKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
-
-
-
-
?
2-aminobenzoyl-ARKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
-
-
-
?
2-aminobenzoyl-IRRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
2-aminobenzoyl-Ile-Arg + Arg-Ala-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
-
-
-
?
2-aminobenzoyl-IRRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
2-aminobenzoyl-Ile-Arg + Arg-Ala-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
-
FRET-substrate, derived from the protein C2 of the classical complement pathway
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
-
FRET-substrate, derived from the protein C2 of the classical complement pathway. Poor substrate
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
-
FRET-substrate, derived from the protein C2 of the classical complement pathway
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
-
FRET-substrate, derived from the protein C2 of the classical complement pathway. Poor substrate
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
Escherichia coli EPEC / E2348/69
-
FRET-substrate, derived from the protein C2 of the classical complement pathway
-
-
?
2-aminobenzoyl-SLGRKIQI-K(N6-2,4-dinitrophenyl)-NH2 + H2O
2-aminobenzoyl-SLGR + KIQI-K(N6-2,4-dinitrophenyl)-NH2
Escherichia coli EPEC / E2348/69
-
FRET-substrate, derived from the protein C2 of the classical complement pathway. Poor substrate
-
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
Abz-SLGR + KIQIK(Dnp)-NH2
-
-
-
-
?
alpha2-antiplasmin + H2O
?
inactivation
-
-
?
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
-
?
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
?
C18G + H2O
?
-
synthetic alpha-helical peptide, whose sequence has been optimized for maximal antibacterial activity
-
-
?
C18G + H2O
?
-
synthetic alpha-helical peptide, whose sequence has been optimized for maximal antibacterial activity
-
-
?
C18G + H2O
?
Escherichia coli EPEC / E2348/69
-
synthetic alpha-helical peptide, whose sequence has been optimized for maximal antibacterial activity
-
-
?
calf thymus histone H2B + H2o
?
-
-
strong fragmentation of histone H2B
-
?
calf thymus histone H3 + H2o
?
-
-
moderate fragmentation of histone H3
-
?
calf thymus histone H4 + H2o
?
-
-
slight fragmentation of histone H4
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
-
OmpT, proteolytic degradation
-
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
-
-
-
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
-
proteolytic degradation
-
-
?
colicin E1 + H2O
?
function in degradation of colicin at the cell surface to protect sensitive cells from infection by colicins suggested
-
-
?
colicin E1 + H2O
?
cleavage by involvement of OmpT proteases determined by SDS-PAGE, processing site determined
-
-
?
dynorphin A + H2O
?
-
proteolytic cleavage, commercial peptide substrate
-
-
?
dynorphin A + H2O
?
cleavage assay of OmpT protease performed with
-
-
?
factor B + H2O
?
-
PgtE generates B fragments of approximately 57 kDa and 28 kDa under non-reducing conditions, while under reducing conditions, the cleavage pattern is different lacking the 28 kDa fragment. PgtE cleaves H near both termini. Mapping of cleavage sites in factor H, overview
-
-
?
factor B + H2O
?
-
PgtE generates B fragments of approximately 57 kDa and 28 kDa under non-reducing conditions, while under reducing conditions, the cleavage pattern is different lacking the 28 kDa fragment. PgtE cleaves H near both termini. Mapping of cleavage sites in factor H, overview
-
-
?
factor H + H2O
?
-
factor H is cleaved at both N- and C-termini, while the central region resists proteolysis
-
-
?
factor H + H2O
?
-
factor H is cleaved at both N- and C-termini, while the central region resists proteolysis
-
-
?
Gelatin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
?
human antiprotease alpha2-antiplasmin + H2O
?
-
involved in infection and pathogenesis
-
-
?
human antiprotease alpha2-antiplasmin + H2O
?
-
inactivation of the substrate by proteolytic cleavage
-
-
?
human circulating complement proteins + H2O
?
-
activation of the substrate
-
-
?
human circulating complement proteins + H2O
?
-
activation of the substrate by proteolytic cleavage
-
-
?
human proenzyme plasminogen + H2O
?
-
low activity of OmpT in activation of the substrate, proteolytic cleavage
-
-
?
human proenzyme plasminogen + H2O
?
-
activation of the substrate by proteolytic cleavage
-
-
?
human proenzyme plasminogen + H2O
?
-
activation of the substrate by proteolytic cleavage
-
-
?
human proenzyme plasminogen + H2O
?
-
involved in pathogenic tissue invasion or nutrition
-
-
?
human single-chain urokinase + H2O
?
-
-
cleavage at the peptide bond Lys158-Ile159, the site cleaved also by the physiological activator human plasmin
-
?
human single-chain urokinase + H2O
?
-
-
cleavage at the peptide bond Lys158-Ile159, the site cleaved also by the physiological activator human plasmin
-
?
human single-chain urokinase + H2O
?
-
-
cleavage at the peptide bond Lys158-Ile159, the site cleaved also by the physiological activator human plasmin
-
?
human single-chain urokinase + H2O
?
-
cleavage at the peptide bond Lys158-Ile159, the site cleaved also by the physiological activator human plasmin. Enzyme addtionally displays activity of EC 3.4.23.48
-
?
human tissue factor pathway inhibitor + H2O
?
-
it is hypothesized that TFPI evolved sensitivity to proteolytic inactivation by bacterial omptins to potentiate procoagulant responses to bacterial infection which may contribute to the hemostatic imbalance in disseminated intravascular coagulation and other coagulopathies accompanying severe sepsis
-
-
?
human tissue factor pathway inhibitor + H2O
?
-
it is hypothesized that TFPI evolved sensitivity to proteolytic inactivation by bacterial omptins to potentiate procoagulant responses to bacterial infection which may contribute to the hemostatic imbalance in disseminated intravascular coagulation and other coagulopathies accompanying severe sepsis
-
-
?
LL-37 + H2O
?
-
human antimicrobial peptide of the cathelicidin family, cleavage occurs at dibasic sites
-
-
?
LL-37 + H2O
?
-
human antimicrobial peptide of the cathelicidin family, cleavage occurs at dibasic sites
-
-
?
LL-37 + H2O
?
Escherichia coli EPEC / E2348/69
-
human antimicrobial peptide of the cathelicidin family, cleavage occurs at dibasic sites
-
-
?
LL37 + H2O
?
a human antimicrobial peptide of the cathelicidin family
-
-
?
LL37 + H2O
?
a human antimicrobial peptide of the cathelicidin family, wild-type LL37 sequence has 2 dibasic sites that can be cleaved by OmpT
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP, rapid, almost complete degradation
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium ATCC 51459
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium ATCC 51459
-
CRAMP, rapid, almost complete degradation
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium DBS 100
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium DBS 100
-
CRAMP, rapid, almost complete degradation
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
CRAMP
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin. PgtE addresses the control systems rather than direct plasminogen activation
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin. PgtE addresses the control systems rather than direct plasminogen activation
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin. PgtE addresses the control systems rather than direct plasminogen activation
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin
-
-
?
T7 RNA polymerase + H2O
?
-
cleavage at Lys-Arg173, Lys-Lys180, and Arg-Lys392
-
-
?
T7 RNA polymerase + H2O
?
-
proteolytic cleavage sites QLNK*RVGHV, HVYK*KAFMQ, and DRAR*KSRRI
-
-
?
TAFI + H2O
TAFIa + ?
TAFI is secreted into plasma as a procarboxypeptidase, it is a regulatory protein linking the coagulation and fibrinolytic systems, and TAFI is protective in septic yersionosis. PptE cleaves at the C-terminal region of TAFI and reduces its activation to TAFIa
-
-
?
TAFI + H2O
TAFIa + ?
cleaves at the C-terminal region of TAFI
-
-
?
tissue factor pathway inhibitor + H2O
?
-
-
-
?
tissue factor pathway inhibitor + H2O
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme PgtE cleaves the tissue factor pathway inhibitor, TFPI
-
-
?
tissue factor pathway inhibitor + H2O
?
-
-
-
?
tissue factor pathway inhibitor + H2O
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme PgtE cleaves the tissue factor pathway inhibitor, TFPI
-
-
?
tissue factor pathway inhibitor + H2O
?
-
-
-
?
tissue factor pathway inhibitor + H2O
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme PgtE cleaves the tissue factor pathway inhibitor, TFPI
-
-
?
WLAAKKGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAAKKGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAARRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAARRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAARRGRG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAARRGRG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAASRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAASRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLARRRGAG + H2O
?
different cleavage sites between OmpP and OmpT protease determined
-
-
?
WLARRRGAG + H2O
?
different cleavage sites between OmpT and OmpP protease determined
-
-
?
WLATRRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLATRRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLRARRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLRARRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLSARRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLSARRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLSERRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLSERRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
ZF-RNase-3 + H2O
?
-
when ZF-RNase-3 is added to Escherichia coli cultures, it is cleaved at a specific Arg-Arg peptide bond, thus engendering two peptide fragments. The larger fragment (residues 31-124), produced by proteolysis and reduction of a disulfide, is recognized as the actual bactericidal agent
-
-
?
ZF-RNase-3 + H2O
?
-
when ZF-RNase-3 is added to Escherichia coli cultures, it is cleaved at a specific Arg-Arg peptide bond, thus engendering two peptide fragments. The larger fragment (residues 31-124), produced by proteolysis and reduction of a disulfide, is recognized as the actual bactericidal agent
-
-
?
additional information
?
-
-
Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs)
-
-
?
additional information
?
-
-
purified enzyme CroP readily cleaves both a synthetic fluorescence resonance energy transfer substrate and the murine cathelicidin-related antimicrobial peptide, while it poorly activates plasminogen into active plasmin
-
-
?
additional information
?
-
Citrobacter rodentium ATCC 51459
-
Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs)
-
-
?
additional information
?
-
Citrobacter rodentium DBS 100
-
Citrobacter rodentium CroP cleaves CRAMP more rapidly than LL-37. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions. By altering the alpha-helicity of LL-37 and CRAMP, decreasing LL-37 alpha-helicity increases its rate of cleavage by CroP. Conversely, increasing CRAMP alpha-helicity decreased its cleavage rate. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs)
-
-
?
additional information
?
-
-
the multifunctional enzyme has virulence-associated functions
-
-
?
additional information
?
-
-
minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme
-
-
?
additional information
?
-
-
not cleaved: insulin B-chain, parathyroid hormone 13-26 and 26-34, small synthetic substrates e.g. Lys-Lys-Leu-Gln-Asp-Val-His-Asn-Phe
-
-
?
additional information
?
-
-
t-butyloxycarbonyl-Leu-Gly-Arg 4-methylcoumarin 7-amide
-
-
?
additional information
?
-
-
endopeptidase specifically recognizing and cleaving consecutive basic residues
-
-
?
additional information
?
-
-
able to process recombinant fusion proteins such as cholesterol esterase/lipase, cholera toxin B subunit, and recombinant Staphylococcus aureus V8 protease derivative, peptides containing an acidic residue at P2 or P2' are not substrates, RD-ELRLYRDHHG is no substrate
-
?
additional information
?
-
-
little or no reaction with aminobenzoylfluorophore-ARIA-(dinitrophenyl)diaminopropionic acid quencher-G and aminobenzoylfluorophore-ARRIA-3-(dinitrophenyl)diaminopropionic acid quencher-G, acetyl-3-(dinitrophenyl)diaminopropionic acid-Ala-Arg-Arg-Ala-Lys(aminobenzoyl)-Gly is no substrate, no hydrolytic activity toward aminobenzoylfluorophore-A-(D)R-(L)R-A-3-(dinitrophenyl)diaminopropionic acid quencher-G, aminobenzoylfluorophore-A-(L)R-(D)R-A-3-(dinitrophenyl)diaminopropionic acid quencher-G and aminobenzoylfluorophore-A-(D)R-(D)R-A-3-(dinitrophenyl)diaminopropionic acid quencher-G
-
?
additional information
?
-
-
activity under extreme denaturing condition
-
-
?
additional information
?
-
-
cleaves peptides between two consecutive basic amino acids
-
?
additional information
?
-
-
cleaves peptides between two consecutive basic amino acids
-
?
additional information
?
-
-
cleaves peptides between two consecutive basic amino acids
-
?
additional information
?
-
-
enzyme is suggested to be involved in urinary tract disease, in DNA excision repair, and in the breakdown of antimicrobial peptides, but its actual biological function remains to be elucidated
-
?
additional information
?
-
-
the enzyme is involved in cell defense and induced production of TNFalpha, especially in clinical isolates, the enzyme is not stimulated by toll-like receptors 2 and 4 signalling
-
-
?
additional information
?
-
-
the multifunctional enzyme has a virulence-associated function in protein degradation
-
-
?
additional information
?
-
-
protein-lipid interactions on model membranes and human mononuclear cells, overview
-
-
?
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
-
-
?
additional information
?
-
OmpT shown to be one of the critical outer membrane protein responsible for chloramphenicol resistance, analysis by comparative proteomics and mutant investigation
-
-
?
additional information
?
-
studies on application of the infectivity-modulated phage display IMOP, applied to determine substrate specificity, protease ompT exemplary tested indicating enrichment of double-arginine motifs, IMOP system shown to improve previous techniques basing on phage display
-
-
?
additional information
?
-
analysis of protease activity for the preferred residues at the cleavage site (P1, P1') and nearest-neighbor positions (P2, P2') and their positional interdependence revealed FRRV as the optimal peptide with the highest OmpT activity. Substituting FRRV into a fragment of LL37, a natural substrate of OmpT, leads to a greater than 400fold improvement in OmpT catalytic efficiency. Wild-type and mutant OmpT display significant differences in their substrate specificities. Substrate consensus sequence screening, substrate specificity, overview. Twelve tetrapeptides display higher activity for wild-type OmpT than does the ARRA peptide, which has an activity of 91.0%, kinetic comparison of peptide substrates that are inserted into the LL37 fragment
-
-
?
additional information
?
-
EHEC OmpT degrades LL-37 and CRAMP at similar rates. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions
-
-
?
additional information
?
-
-
EHEC OmpT degrades LL-37 and CRAMP at similar rates. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions
-
-
?
additional information
?
-
Escherichia coli EDL933
EHEC OmpT degrades LL-37 and CRAMP at similar rates. Comparison of the substrate specificity and substrate sequence specificity of the omptins OmpT from Escherichia coli and CroP from Citrobacter rodentium. The enzymes have the same preference for cleaving at dibasic sites, but show important difference in substrate recognition, overview. LL-37 is alpha-helical and CRAMP is unstructured under the experimental conditions
-
-
?
additional information
?
-
-
enzyme displays restriction of catalysis at the S1 subsite, with a preference for lysine, arginine, leucine, tyrosine, and phenylalanine residues. No hydrolysis of the substrate peptide is observed with amino acids A, D, E, H, I, M, N, P, Q, S, T, V, or W in the S1 position. At S2 and S1' subsites, the enzyme exhibits a good acceptance of amino acids L, M, E, D, R and S, Y, Q, respectively
-
-
?
additional information
?
-
-
the enzyme is important in the intracellular phases of salmonellosis, the multifunctional enzyme has virulence-associated functions
-
-
?
additional information
?
-
-
minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme
-
-
?
additional information
?
-
substrate specificity of PgtE, determination of cleavage sites and sequences, overview
-
-
?
additional information
?
-
-
PgtE cleaves both B and H, whereas its close homologue Pla of Yersinia pestis (EC 3.4.23.48) cleaves only H
-
-
?
additional information
?
-
-
PgtE cleaves both B and H, whereas its close homologue Pla of Yersinia pestis (EC 3.4.23.48) cleaves only H
-
-
?
additional information
?
-
-
the enzyme is important in the intracellular phases of shigellosis, the multifunctional enzyme has virulence-associated functions
-
-
?
additional information
?
-
-
minor sequence variations in the surface loops near the catalytic residue have profound effects on the target specificity of the enzyme
-
-
?
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
-
-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha2-antiplasmin + H2O
?
inactivation
-
-
?
ColE2-Im2 protein complex + H2O
?
-
a small amount of the endonuclease colicin E2 associated with the cognate immunity protein Im2, is susceptible to proteolytic cleavage by omptin. The presence of outer membrane protein BtuB is required for ColE-Im2 cleavage by omptin. The amount of colicin cleaved is greatly enhanced when ColE2 is dissociated from Im2. Omptin cleaves the C-terminal DNase domain of the toxin. Strains that over-produce OmpT are less susceptible to infection by ColE2 than by ColE2-Im2
-
-
?
colicin E1 + H2O
?
function in degradation of colicin at the cell surface to protect sensitive cells from infection by colicins suggested
-
-
?
gelatine + H2O
?
degradation
-
-
?
human antiprotease alpha2-antiplasmin + H2O
?
-
involved in infection and pathogenesis
-
-
?
human circulating complement proteins + H2O
?
-
activation of the substrate
-
-
?
human plasminogen + H2O
?
-
proteolytic cleavage site CPGR*VVGGC, activation
-
-
?
LL37 + H2O
?
a human antimicrobial peptide of the cathelicidin family
-
-
?
plasminogen activator inhibitor-1 + H2O
?
inactivation
-
-
?
small-molecular-weight chromogenic peptides + H2O
?
-
OmpT, proteolytic cleavage
-
-
?
TAFI + H2O
TAFIa + ?
TAFI is secreted into plasma as a procarboxypeptidase, it is a regulatory protein linking the coagulation and fibrinolytic systems, and TAFI is protective in septic yersionosis. PptE cleaves at the C-terminal region of TAFI and reduces its activation to TAFIa
-
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
-
OmpT, proteolytic degradation
-
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
-
-
-
-
?
factor H + H2O
?
-
factor H is cleaved at both N- and C-termini, while the central region resists proteolysis
-
-
?
factor H + H2O
?
-
factor H is cleaved at both N- and C-termini, while the central region resists proteolysis
-
-
?
human proenzyme plasminogen + H2O
?
-
low activity of OmpT in activation of the substrate, proteolytic cleavage
-
-
?
human proenzyme plasminogen + H2O
?
-
activation of the substrate by proteolytic cleavage
-
-
?
human proenzyme plasminogen + H2O
?
-
involved in pathogenic tissue invasion or nutrition
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium ATCC 51459
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
Citrobacter rodentium DBS 100
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
CRAMP
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin. PgtE addresses the control systems rather than direct plasminogen activation
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin. PgtE addresses the control systems rather than direct plasminogen activation
-
-
?
plasminogen + H2O
plasmin + ?
activation, but PgtE does not catalyze formation of stable plasmin activity because it cleaves also the B chain of plasmin. PgtE addresses the control systems rather than direct plasminogen activation
-
-
?
tissue factor pathway inhibitor + H2O
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme PgtE cleaves the tissue factor pathway inhibitor, TFPI
-
-
?
tissue factor pathway inhibitor + H2O
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme PgtE cleaves the tissue factor pathway inhibitor, TFPI
-
-
?
tissue factor pathway inhibitor + H2O
?
TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme PgtE cleaves the tissue factor pathway inhibitor, TFPI
-
-
?
additional information
?
-
-
the multifunctional enzyme has virulence-associated functions
-
-
?
additional information
?
-
-
activity under extreme denaturing condition
-
-
?
additional information
?
-
-
cleaves peptides between two consecutive basic amino acids
-
?
additional information
?
-
-
cleaves peptides between two consecutive basic amino acids
-
?
additional information
?
-
-
cleaves peptides between two consecutive basic amino acids
-
?
additional information
?
-
-
enzyme is suggested to be involved in urinary tract disease, in DNA excision repair, and in the breakdown of antimicrobial peptides, but its actual biological function remains to be elucidated
-
?
additional information
?
-
-
the enzyme is involved in cell defense and induced production of TNFalpha, especially in clinical isolates, the enzyme is not stimulated by toll-like receptors 2 and 4 signalling
-
-
?
additional information
?
-
-
the multifunctional enzyme has a virulence-associated function in protein degradation
-
-
?
additional information
?
-
-
the enzyme is important in the intracellular phases of salmonellosis, the multifunctional enzyme has virulence-associated functions
-
-
?
additional information
?
-
-
PgtE cleaves both B and H, whereas its close homologue Pla of Yersinia pestis (EC 3.4.23.48) cleaves only H
-
-
?
additional information
?
-
-
PgtE cleaves both B and H, whereas its close homologue Pla of Yersinia pestis (EC 3.4.23.48) cleaves only H
-
-
?
additional information
?
-
-
the enzyme is important in the intracellular phases of shigellosis, the multifunctional enzyme has virulence-associated functions
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
metal ion docking studies, Mg2+ has better interaction with enzyme PgtE compared to Zn2+ and Cu2+ ions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
calf thymus histone H2B
-
growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 3.8 microM. Histone H2B penetrates the cell membrane of JCM5491 OmpT+ cells
-
calf thymus histone H3
-
growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 10 microM. Histones H3 and H4 remain on the cell surface and subsequently disrupt the cell membrane structure with bleb formation in a manner similar to general antimicrobial peptides
-
calf thymus histone H4
-
growth inhibitory activity against bacterial gene expressing Escherichia coli with calculated 50% growth inhibitory concentrations of 12.7 microM. Histones H3 and H4 remain on the cell surface and subsequently disrupt the cell membrane structure with bleb formation in a manner similar to general antimicrobial peptides
-
Aprotinin
-
classical protease inhibitors are ineffective against CroP activity, but the serine protease inhibitor aprotinin displays inhibitory potency in the micromolar range. Aprotinin acts as a competitive inhibitor of CroP activity and interferes with the cleavage of the murine cathelicidin-related antimicrobial peptide. Structural model of the aprotinin-omptin complex in which Lys15 of aprotinin forms salt bridges with conserved negatively charged residues of the omptin active site, molecular docking, overview. Aprotinin inhibits CRAMP proteolytic degradation by CroP. Docking model of the aprotinin-omptin complex. Lys15 of aprotinin interacts with Glu27 and Asp208 (OmpT numbering), which are the two negatively charged residues that form the S1 specificity pocket of omptins
Aprotinin
ability of EHEC EDL933 cells to cleave the FRET substrate in the presence of increasing concentrations of aprotinin, about 90% inhibition at 0.2 mM. Docking model of the aprotinin-omptin complex. Lys15 of aprotinin interacts with Glu27 and Asp208 (OmpT numbering), which are the two negatively charged residues that form the S1 specificity pocket of omptin
diisopropylfluorophosphate
-
significant inhibition only at high concentrations
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
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
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
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
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
additional information
molecular docking study with protease inhibitors, overview. No interaction with lopinavir and tipranavir
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Escherichia coli lipopolysaccharide
-
LPS, required for omptin activity
-
Urea
-
optimal concentration: 4-5 M, inclusion bodies from Escherichia coli as substrate
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
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
lipopolysaccharide
OmpT protein active only in the presence of
lipopolysaccharide
purified OmpP protease active only in the presence of, similar to OmpT protein homologue
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
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
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
lipopolysaccharides
-
e.g. LPS K12, required for activity, lipid-protein interactions, complex activity analysis on model membranes and human mononuclear cells, overview
-
lipopolysaccharides
-
required for activity, protein-lipid interactions, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.052
2-aminobenzoyl-AKKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.0083
2-aminobenzoyl-AKRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.0104
2-aminobenzoyl-ARKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.0031
2-aminobenzoyl-ARRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.0036
2-aminobenzoyl-IRRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.00064
2-aminobenzoyl-KLKSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
0.00024
2-aminobenzoyl-KLRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
0.0003
2-aminobenzoyl-KMRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
0.00043
2-aminobenzoyl-KNRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
0.00012
2-aminobenzoyl-KQRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
0.0013
2-aminobenzoyl-RRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
0.0225
Ac-GLLGDFARRAKEKIGC
pH and temperature not specified in the publication
0.0184
Ac-GLLGDFFRKSKEKIGC
pH and temperature not specified in the publication
0.0094
Ac-GLLGDFFRRVKEKIGC
pH and temperature not specified in the publication
additional information
additional information
-
kinetics for phage display generated peptide substrates, overview
-
0.53
IAA-Arg-Arg-p-nitroanilide
-
pH 6.5, 37°C, wild-type, purified from outer membrane
0.58
IAA-Arg-Arg-p-nitroanilide
-
pH 6.5, 37°C, wild-type, recombinant expressed
0.0003
o-aminobenzoyl-Ala-Arg-Arg-Ala-3-nitrotyrosine-NH2
-
pH 6.5, 37°C, wild-type, purified from outer membrane
0.0004
o-aminobenzoyl-Ala-Arg-Arg-Ala-3-nitrotyrosine-NH2
-
pH 6.5, 37°C, wild-type, recombinant expressed
0.0011
o-aminobenzoyl-Ala-Arg-Arg-Ala-3-nitrotyrosine-NH2
-
pH 6.5, 37°C, variant G216K/K217G
0.023
WEEGGRRIGRGGK
used as a control substrate for determination of the activity of OmpT protease
0.055
WEEGGRRIGRGGK
used as a control substrate for determination of the activity of OmpT protease
0.008
WLARRRGAG
different cleavage sites used by OmpP or OmpT proteases
0.19
WLARRRGAG
different cleavage sites used by OmpP or OmpT proteases
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2380
2-aminobenzoyl-AKKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
738
2-aminobenzoyl-AKRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
612
2-aminobenzoyl-ARKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
192
2-aminobenzoyl-ARRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
84
2-aminobenzoyl-IRRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
1.54
2-aminobenzoyl-KLKSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
1.15
2-aminobenzoyl-KLRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
0.64
2-aminobenzoyl-KMRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
0.8
2-aminobenzoyl-KNRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
0.824
2-aminobenzoyl-KQRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
78
2-aminobenzoyl-RRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
12.9
Ac-GLLGDFARRAKEKIGC
pH and temperature not specified in the publication
0.3
Ac-GLLGDFFRKSKEKIGC
pH and temperature not specified in the publication
57.6
Ac-GLLGDFFRRVKEKIGC
pH and temperature not specified in the publication
2400
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly
-
pH 8.3, 37°C
24
IAA-Arg-Arg-p-nitroanilide
-
pH 6.5, 37°C, wild-type, purified from outer membrane and wild-type, recombinant expressed
96
o-aminobenzoyl-Ala-Arg-Arg-Ala-3-nitrotyrosine-NH2
-
pH 6.5, 37°C, variant G216K/K217G
2280
o-aminobenzoyl-Ala-Arg-Arg-Ala-3-nitrotyrosine-NH2
-
pH 6.5, 37°C, wild-type, purified from outer membrane
2460
o-aminobenzoyl-Ala-Arg-Arg-Ala-3-nitrotyrosine-NH2
-
pH 6.5, 37°C, wild-type, recombinant expressed in Escherichia coli
3.4
WEEGGRRIGRGGK
used as a control substrate for determination of the activity of OmpT protease
8.8
WEEGGRRIGRGGK
used as a control substrate for determination of the activity of OmpT protease
1.2
WLARRRGAG
different cleavage sites used by OmpP or OmpT proteases
2.2
WLARRRGAG
different cleavage sites used by OmpP or OmpT proteases
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2406
2-aminobenzoyl-KLKSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
2133
2-aminobenzoyl-KMRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
1860
2-aminobenzoyl-KNRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
2000
2-aminobenzoyl-KQRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
573.3
Ac-GLLGDFARRAKEKIGC
pH and temperature not specified in the publication
16.3
Ac-GLLGDFFRKSKEKIGC
pH and temperature not specified in the publication
6127.7
Ac-GLLGDFFRRVKEKIGC
pH and temperature not specified in the publication
4732
2-aminobenzoyl-KLRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
4792
2-aminobenzoyl-KLRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 4.5, 40°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.019
2-aminobenzoyl-A-(L)R-(D)R-A-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly
-
pH 8.3, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
comparative proteome analysis of chloramphenicol-resistant Escherichia coli, two-dimensional electrophoresis, MALDI-TOF mass spectroscopy and Western blotting performed, differential protein expression profiles with and without chloramphenicol treatment shown, antimicrobial susceptibility tested, OmpT protease identified as critically altered protein in chloramphenicol-resistant Escherichia coli, mutant analysis performed
additional information
effects of OmpT protease on colony-forming ability and production of fibrous protein polymers determined, involvement of OmpT protease in protein quality control within the cell discussed
additional information
phage display applied to analyse substrate specificity of OmpP protease in comparison to OmpT protease, different substrate specificities between OmpP and OmpT proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
phage display applied to analyse substrate specificity of OmpP protease in comparison to OmpT protease, different substrate specificities between OmpP and OmpT proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
-
phage display applied to analyse substrate specificity of OmpP protease in comparison to OmpT protease, different substrate specificities between OmpP and OmpT proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
phage display applied to analyse substrate specificity of OmpT protease in comparison to OmpP protease, different substrate specificities between OmpT and OmpP proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
phage display applied to analyse substrate specificity of OmpT protease in comparison to OmpP protease, different substrate specificities between OmpT and OmpP proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
-
phage display applied to analyse substrate specificity of OmpT protease in comparison to OmpP protease, different substrate specificities between OmpT and OmpP proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined
additional information
strains expressing OmpT protease shown to cleave colicin E1 at the residues K84 and K95 in the N-terminal translocation domain, leading to the removal of the TolQA box essential for cytotoxicity of colicin E1, in vivo data indicating effects of OmpT protease on colicin E1 cell-killing activity shown
additional information
structural and functional relationships for wild-type and mutated OmpT proteins investigated, relevant case of the Michaelis complex of the outer-membrane protease T (OmpT) analyzed by a hybrid molecular mechanics/coarse-grained (MM/CG) approach, structural explanation for decreased catalytic activity of the mutants S99A and H212A given
additional information
-
structural and functional relationships for wild-type and mutated OmpT proteins investigated, relevant case of the Michaelis complex of the outer-membrane protease T (OmpT) analyzed by a hybrid molecular mechanics/coarse-grained (MM/CG) approach, structural explanation for decreased catalytic activity of the mutants S99A and H212A given
additional information
studies on development of a new substrate phage system, construction of a random hexapeptide library described, selection of the phage display library with OmpT protease to demonstrate application of the infectivity-modulated phage display IMOP
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
additional information
-
proteolytic cleavage observed only under neutral conditions
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
CroP exhibits robust activity over a pH range of 6.0 to 8.0, with optimal activity at pH 7.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the rough variant 14028R is resistant to a smooth LPS-specific bacteriophage P22c2
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
29795, 29796, 29797, 29798, 29799, 29800, 650046, 650422, 650633, 650667, 650983, 651090, 651289, 660757, 661351, 661616, 661904, 663249
-
-
brenda
the rough variant 14028R is resistant to a smooth LPS-specific bacteriophage P22c2
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
integral membrane protease, outer membrane, membrane bound
brenda
-
dimyristoylphosphatidylcholine lipid bilayer embedded beta-barrel
brenda
-
enzyme incorporation mechanism into membranes, overview
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
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
-
malfunction
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
-
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
-
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
-
physiological function
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
-
additional information
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
Show AA Sequence and Transmembrane Helices (263 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
180000
33500
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
conformational flexibility of the outer membrane embedded enzyme, molecular dynamic simulation, overview
additional information
-
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of the structure of Pla and the modeled structure of protease Epo of the plant pathogenic Erwinia pyrifoliae
-
hanging drop vapour diffusion method, space group P3(2)21, unit cell parameters a : B : 98.39 A, c : 165.70 A
-
PDB 1I78 crystal structure analysis with reversal of mutations A99S, K261G, and G217K required for crystallization
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D208A
-
introduced as silent mutation in plasmids, transformation with plasmids
D208G
-
site-directed mutagenesis, the mutant enzyme shows increased specificity for the A-R cleavage site compared to the wild-type enzyme
D210A
-
introduced as silent mutation in plasmids, transformation with plasmids
D43A
-
introduced as silent mutation in plasmids, transformation with plasmids
D83A
-
introduced as silent mutation in plasmids, transformation with plasmids
D85A
-
introduced as silent mutation in plasmids, transformation with plasmids
D97A
D97C
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97F
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97H
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, preference for human calcitonin precursor, substrate specificity with fusion protein, overview
D97L
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, preference for human adrenocarticotropic hormone, substrate specificity with fusion protein, overview
D97M
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, preference for a fusion peptide substrate with the sequence R-R-R-A-R*-motilin, substrate specificity with fusion protein, overview
D97N
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97Q
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97S
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97T
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
E111A
-
introduced as silent mutation in plasmids, transformation with plasmids
E136A
-
introduced as silent mutation in plasmids, transformation with plasmids
E193A
-
introduced as silent mutation in plasmids, transformation with plasmids
E250A
-
introduced as silent mutation in plasmids, transformation with plasmids
E27A
-
introduced as silent mutation in plasmids, transformation with plasmids
G216K/K217G
S223R
-
site-directed mutagenesis, the mutant enzyme shows increased specificity for the A-R cleavage site and overall reduced activity compared to the wild-type enzyme
S99A/G216K/K217G
-
recombinant ompT variant in order to abolish autoproteolysis
D206A
additional information
D97A
-
introduced as silent mutation in plasmids, transformation with plasmids
D97A
-
site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
G216K/K217G
-
recombinant ompT variant in order to abolish autoproteolysis
G216K/K217G
site-directed mutagenesis, mutation to remove the dibasic proteolysis site. The mutant has a circa 30% lower activity than wild-type OmpT
D206A
-
site-directed mutagenesis, inacticve catalytic site mutant
D206A
-
site-directed mutagenesis, inacticve catalytic site mutant
-
additional information
-
generation of a Citrobacter rodentium DELTAcroP strain
additional information
Citrobacter rodentium ATCC 51459
-
generation of a deletion mutant DELTAcroP
-
additional information
-
swapping of ten amino acid residues at two surface loops of Pla and membrane protease Epo of the plant pathogenic Erwinia pyrifoliae introduces plasminogen activation capacity in Epo and inactivates the function in Pla
additional information
-
random mutagenesis of gene ompT, screening for mutant variants with altered cleavage specificity, e.g. mutant variants 1.2.19 and 1.3.19 exhibits higher specificity for the cleavage site A-R and lower specificity for R-R than the wild-type
additional information
complementation of strain BL21 producing fusion protein GST-Sup35NM with the wild-type OmpT-gene restores colony-forming ability
additional information
referring to the classical Lpp-OmpA (LOA) display system, the signal peptide and nine amino acids of the mature outer membrane prolipoprotein Lpp are fused to the transmembrane domain comprising five beta-strands of truncated OmpT to generate a Lpp-OmpT (LOT) display system. The C-terminal fusion strategy is used to fuse a small peptide (His tag) and red fluorescent protein (mCherry) to the C-terminus of LOT. Exposed histidine tags present in recombinant proteins form complexes with transition metal ions such as Ni2+, Zn2+, Cu2+, and Fe3+. Adsorption analysis of cells expressing the chimeric mutant protein using Cu2+, adhesion of surface engineered cells to Cu2+-chelating sepharose beads, method evaluation, overview
additional information
-
referring to the classical Lpp-OmpA (LOA) display system, the signal peptide and nine amino acids of the mature outer membrane prolipoprotein Lpp are fused to the transmembrane domain comprising five beta-strands of truncated OmpT to generate a Lpp-OmpT (LOT) display system. The C-terminal fusion strategy is used to fuse a small peptide (His tag) and red fluorescent protein (mCherry) to the C-terminus of LOT. Exposed histidine tags present in recombinant proteins form complexes with transition metal ions such as Ni2+, Zn2+, Cu2+, and Fe3+. Adsorption analysis of cells expressing the chimeric mutant protein using Cu2+, adhesion of surface engineered cells to Cu2+-chelating sepharose beads, method evaluation, overview
additional information
-
construction of Salmonella enterica mutant DELTApgtE strain 14028R-1 from the isogenic virulent wild-type strain 14028R. Mutant strain 14028R-1 is inactive with factor H and B. Complementation of 14028R-1 with pgtE-encoding pMRK3 recovers the activity toward B and H
additional information
-
construction of Salmonella enterica mutant DELTApgtE strain 14028R-1 from the isogenic virulent wild-type strain 14028R. Mutant strain 14028R-1 is inactive with factor H and B. Complementation of 14028R-1 with pgtE-encoding pMRK3 recovers the activity toward B and H
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
-
ompT is associated in inclusion bodies and active in the presence of high concentrations
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, gel filtration and SDS-PAGE
recombinant wild-type enzyme CroP from DELTAcroP-deletion mutant strain of Citrobacter rodentium crude extract by detergent solubilization, ultracentrifugation, anion exchange chromatography, and dialysis
-
recombinant protein, gel filtration and SDS-PAGE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21, mutation in OmpT protein characterized in BL21 producing fusion protein GST-Sup35NM
expressed in Escherichia coli XL1-Blue, additional strains and plasmids listed, construction of phage libraries and substrate phage described
expression in Escherichia coli
gene croP, recombinant expression of wild-type enzyme in DELTAcroP-deletion mutant strain of Citrobacter rodentium
-
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
-
gene ompT, phage display metod used for substrate specificity analysis, expression in Escherichia coli AN1 cells
-
gene pgtE, DNA and amino acid sequence determination and analysis
gene pla is 9.5 kb plasmid pPCP1 encoded, phylogenetic tree of the omptin family
-
inserted into pTrc99A, expressed in Escherichia coli, additional strains and plasmids of the study listed
overexpressed without its signal sequence in Escherichia coli K-12 strain DH5alpha using a T7 system
-
recombinant expression of the chimeric C-terminally His-tagged and mCherry fluorescence-tagged surface anchor Lpp-OmpT (LOT) in Escherichia coli strain BL21(DE3)
recombinant expression of wild-type pgtE in Escherichia coli strain 83972 DELTAompT, which is deleted for the endogenous omptin gene ompT and lacks ompP. Escherichia coli strain 83972 DELTAompT expressing PgtE cleaves B in a time-dependent fashion generating four immunoreactive fragments
-
the gene pgtE is encoded on the chromosome, phylogenetic tree of the omptin family
-
the gene plaA is 36 kb plasmid pEP36 encoded, phylogenetic tree of the omptin family
-
the gene sopA is 210 kb virulence plasmid pWR100-encoded, phylogenetic tree of the omptin family
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
croP trancription is reduced in DELTAPhoPQ (two-component system composed of the sensor kinase PhoQ and the cognate response regulator PhoP), indicating that croP expression is partly under under the control of PhoP
expression of the ompT gene is higher in EHEC strains than in EPEC strains
PgtE of Salmonella enterica is not expressed under normal laboratory conditions, but the transcription of pgtE is high in mouse macrophages where the degradation of alpha2AP by Salmonella enterica cells also is high. Expression of PgtE is regulated by the SlyA regulator
expression of the ompT gene is higher in EHEC strains than in EPEC strains
-
expression of the ompT gene is higher in EHEC strains than in EPEC strains
-
-
expression of the ompT gene is higher in EHEC strains than in EPEC strains
Escherichia coli EPEC / E2348/69
-
-
PgtE of Salmonella enterica is not expressed under normal laboratory conditions, but the transcription of pgtE is high in mouse macrophages where the degradation of alpha2AP by Salmonella enterica cells also is high. Expression of PgtE is regulated by the SlyA regulator
PgtE of Salmonella enterica is not expressed under normal laboratory conditions, but the transcription of pgtE is high in mouse macrophages where the degradation of alpha2AP by Salmonella enterica cells also is high. Expression of PgtE is regulated by the SlyA regulator
-
-
PgtE of Salmonella enterica is not expressed under normal laboratory conditions, but the transcription of pgtE is high in mouse macrophages where the degradation of alpha2AP by Salmonella enterica cells also is high. Expression of PgtE is regulated by the SlyA regulator
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
food industry
-
the peptidase shows maximal milk clotting activity at 60-65 °C and maintenance of enzymatic activity above 80% in the presence of 20 mM CaCl2
medicine
pharmacology
studies on treatment of infection by antibiotic-resistant bacteria
biotechnology
-
engineering of enzyme variants with targeted, high substrate specificity
biotechnology
-
utilization of outer-membrane endoprotease OmpT variants as processing enzymes for production of peptides from designer fusion proteins, e.g. useful in motilin production, overview
biotechnology
-
OmpT protease could be a possible factor responsible for reducing the expression of GFP at 37°C for wildtype GFP clone in K12 hosts like DH5alpha, JM109, LE 392
medicine
-
use in therapeutic peptide production, efficient cleavage of substrates with basic amino acids at the P4 and P6 positions, able to cleave efficiently a fusion protein carrying human glucagon-like peptide I, releases mature protein from an Escherichia coli expressed fusion protein carrying human atrial natriuretic peptide, a drug for acute congestive heart failure
medicine
-
the different contributions of EHEC and EPEC strains OmpT to the degradation and inactivation of antimicrobial peptide LL-37 may be due to their adaptation to their respective niches within the host, the colon and small intestine, respectively, where the environmental cues and abundance of antimicrobial peptides are different
medicine
the enzyme is a target for vaccine development. B-cell epitope mapping with human sera, three-dimensional modeling, omptins allergenicity and antigenicity prediction, overview
medicine
the enzyme is a target for vaccine development. B-cell epitope mapping with human sera, three-dimensional modeling, omptins allergenicity and antigenicity prediction, overview
medicine
-
the enzyme is a target for vaccine development. B-cell epitope mapping with human sera, three-dimensional modeling, omptins allergenicity and antigenicity prediction, overview
-
medicine
-
the enzyme is a target for vaccine development. B-cell epitope mapping with human sera, three-dimensional modeling, omptins allergenicity and antigenicity prediction, overview
-
medicine
-
the different contributions of EHEC and EPEC strains OmpT to the degradation and inactivation of antimicrobial peptide LL-37 may be due to their adaptation to their respective niches within the host, the colon and small intestine, respectively, where the environmental cues and abundance of antimicrobial peptides are different
-
medicine
Escherichia coli EPEC / E2348/69
-
the different contributions of EHEC and EPEC strains OmpT to the degradation and inactivation of antimicrobial peptide LL-37 may be due to their adaptation to their respective niches within the host, the colon and small intestine, respectively, where the environmental cues and abundance of antimicrobial peptides are different
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sugimura, K.; Nishihara, T.
Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues: identity of protease VII and OmpT
J. Bacteriol.
170
5625-5632
1988
Escherichia coli
brenda
Hanke, C.; Hess, J.; Schumacher, G.; Goebel, W.
Processing by OmpT of fusion proteins carrying the HlyA transport signal during secretion by the Escherichia coli hemolysin transport system
Mol. Gen. Genet.
233
42-48
1992
Escherichia coli
brenda
Grodberg, J.; Lundrigan, M.D.; Toledo, D.L.; Mangel, W.F.; Dunn, J.J.
Complete nucleotide sequence and deduced amino acid sequence of the ompT gene of Escherichia coli K-12
Nucleic Acids Res.
16
1209
1988
Escherichia coli
brenda
Mangel, W.F.; Toledo, D.L.; Brown, M.T.; Worzalla, K.; Lee, M.; Dunn, J.J.
Omptin: an Escherichia coli outer membrane proteinase that activates plasminogen
Methods Enzymol.
244
384-399
1994
Escherichia coli
brenda
White, C.B.; Chen, Q.; Kenyon, G.L.; Babbitt, P.C.
A novel activity of OmpT. Proteolysis under extreme denaturing conditions
J. Biol. Chem.
270
12990-12994
1995
Escherichia coli
brenda
Zhao, G.P.; Somerville, R.L.
An amino acid switch (Gly281-->Arg) within the hinge region of the tryptophan synthase beta subunit creates a novel cleavage site for the OmpT protease and selectively diminishes affinity toward a specific monoclonal antibody
J. Biol. Chem.
268
14912-14920
1993
Escherichia coli
brenda
Dekker, N.; Cox, R.C.; Kramer, R.A.; Egmond, M.R.
Substrate specificity of the integral membrane protease ompT determined by spatially addressed peptide libraries
Biochemistry
40
1694-1701
2001
Escherichia coli
brenda
Goldberg, M.D.; Canvin, J.R.; Freestone, P.; Andersen, C.; Laoudj, D.; Williams, P.H.; Holland, I.B.; Norris, V.
Artifactual cleavage of E. coli H-NS by OmpT
Biochimie
79
315-322
1997
Escherichia coli
brenda
Okuno, K.; Yabuta, M.; Kawanishi, K.; Ohsuye, K.; Ooi, T.; Kinoshita, S.
Substrate specificity at the P1' site of Escherichia coli OmpT under denaturing conditions
Biosci. Biotechnol. Biochem.
66
127-134
2002
Escherichia coli, no activity in Escherichia coli, no activity in Escherichia coli W3110 / ATCC 27325
brenda
Okuno, K.; Yabuta, M.; Ohsuye, K.; Ooi, T.; Kinoshita, S.
An analysis of target preferences of Escherichia coli outer-membrane endoprotease OmpT for use in therapeutic peptide production: efficient cleavage of substrates with basic amino acids at the P4 and P6 positions
Biotechnol. Appl. Biochem.
36
77-84
2002
Escherichia coli, no activity in Escherichia coli, no activity in Escherichia coli W3110 / ATCC 27325
brenda
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
EMBO J.
20
5033-5039
2001
Escherichia coli
brenda
Kramer, R.A.; Zandwijken, D.; Egmond, M.R.; Dekker, N.
In vitro folding, purification and characterization of Escherichia coli outer membrane protease OmpT
Eur. J. Biochem.
267
885-893
2000
Escherichia coli
brenda
Kramer, R.A.; Vandeputte-Rutten, L.; de Roon, G.J.; Gros, P.; Dekker, N.; Egmond, M.R.
Identification of essential acidic residues of outer membrane protease OmpT supports a novel active site
FEBS Lett.
505
426-430
2001
Escherichia coli
brenda
Okuno, K.; Yabuta, M.; Ooi, T.; Kinoshita, S.
Utilization of Escherichia coli outer-membrane endoprotease OmpT variants as processing enzymes for production of peptides from designer fusion proteins
Appl. Environ. Microbiol.
70
76-86
2004
Escherichia coli
brenda
Baaden, M.; Sansom, M.S.
OmpT: molecular dynamics simulations of an outer membrane enzyme
Biophys. J.
87
2942-2953
2004
Escherichia coli
brenda
Brandenburg, K.; Garidel, P.; Schromm, A.B.; Andra, J.; Kramer, A.; Egmond, M.; Wiese, A.
Investigation into the interaction of the bacterial protease OmpT with outer membrane lipids and biological activity of OmpT:lipopolysaccharide complexes
Eur. Biophys. J.
34
28-41
2005
Escherichia coli
brenda
Kukkonen, M.; Korhonen, T.K.
The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis
Int. J. Med. Microbiol.
294
7-14
2004
Escherichia coli, Salmonella enterica, Yersinia pestis, Shigella flexneri, Erwinia pyrifoliae
brenda
McCarter, J.D.; Stephens, D.; Shoemaker, K.; Rosenberg, S.; Kirsch, J.F.; Georgiou, G.
Substrate specificity of the Escherichia coli outer membrane protease OmpT
J. Bacteriol.
186
5919-5925
2004
Escherichia coli K-12
brenda
Varadarajan, N.; Gam, J.; Olsen, M.J.; Georgiou, G.; Iverson, B.L.
Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity
Proc. Natl. Acad. Sci. USA
102
6855-6860
2005
Escherichia coli
brenda
Neri, M.; Baaden, M.; Carnevale, V.; Anselmi, C.; Maritan, A.; Carloni, P.
Microseconds dynamics simulations of the outer-membrane protease T
Biophys. J.
94
71-78
2008
Escherichia coli (P09169), Escherichia coli
brenda
Ono, B.; Kimiduka, H.; Kubota, M.; Okuno, K.; Yabuta, M.
Role of the ompT mutation in stimulated decrease in colony-forming ability due to intracellular protein aggregate formation in Escherichia coli strain BL21
Biosci. Biotechnol. Biochem.
71
504-512
2007
Escherichia coli (P09169)
brenda
Chaparro-Riggers, J.F.; Breves, R.; Maurer, K.H.; Bornscheuer, U.
Modulation of infectivity in phage display as a tool to determine the substrate specificity of proteases
Chembiochem
7
965-970
2006
Escherichia coli (P09169)
brenda
Masi, M.; Vuong, P.; Humbard, M.; Malone, K.; Misra, R.
Initial steps of colicin E1 import across the outer membrane of Escherichia coli
J. Bacteriol.
189
2667-2676
2007
Escherichia coli (P09169)
brenda
Hwang, B.Y.; Varadarajan, N.; Li, H.; Rodriguez, S.; Iverson, B.L.; Georgiou, G.
Substrate specificity of the Escherichia coli outer membrane protease OmpP
J. Bacteriol.
189
522-530
2007
Escherichia coli (P09169), Escherichia coli (P34210), Escherichia coli
brenda
Li, H.; Lin, X.M.; Wang, S.Y.; Peng, X.X.
Identification and antibody-therapeutic targeting of chloramphenicol-resistant outer membrane proteins in Escherichia coli
J. Proteome Res.
6
3628-3636
2007
Escherichia coli (P09169)
brenda
Duche, D.; Issouf, M.; Lloubes, R.
Immunity protein protects colicin E2 from OmpT protease
J. Biochem.
145
95-101
2009
Escherichia coli
brenda
Duret, G.; Delcour, A.H.
Size and dynamics of the Vibrio cholerae porins OmpU and OmpT probed by polymer exclusion
Biophys. J.
98
1820-1829
2010
Vibrio cholerae serotype O1
brenda
Yun, T.; Cott, J.; Tapping, R.; Slauch, J.; Morrissey, J.
Proteolytic inactivation of tissue factor pathway inhibitor by bacterial omptins
Blood
113
1139-1148
2009
Escherichia coli, Salmonella enterica
brenda
Zanfardino, A.; Pizzo, E.; Di Maro, A.; Varcamonti, M.; DAlessio, G.
The bactericidal action on Escherichia coli of ZF-RNase-3 is triggered by the suicidal action of the bacterium OmpT protease
FEBS J.
277
1921-1928
2010
Escherichia coli DH5[alpha], Escherichia coli DH5-alpha
brenda
Salunkhe, S.S.; Raiker, V.A.; Rewanwar, S.; Kotwal, P.; Kumar, A.; Padmanabhan, S.
Enhanced fluorescent properties of an OmpT site deleted mutant of green fluorescent protein
Microb. Cell Fact.
9
26
2010
Escherichia coli
brenda
Le Sage, V.; Zhu, L.; Lepage, C.; Portt, A.; Viau, C.; Daigle, F.; Gruenheid, S.; Le Moual, H.
An outer membrane protease of the omptin family prevents activation of the Citrobacter rodentium PhoPQ two-component system by antimicrobial peptides
Mol. Microbiol.
74
98-111
2009
Citrobacter rodentium ICC168 (D2TNS3)
brenda
Haiko, J.; Laakkonen, L.; Westerlund-Wikstroem, B.; Korhonen, T.K.
Molecular adaptation of a plant-bacterium outer membrane protease towards plague virulence factor Pla
BMC Evol. Biol.
11
43
2011
Erwinia pyrifoliae
brenda
Thomassin, J.L.; Brannon, J.R.; Gibbs, B.F.; Gruenheid, S.; Le Moual, H.
OmpT outer membrane proteases of enterohemorrhagic and enteropathogenic Escherichia coli contribute differently to the degradation of Human LL-37
Infect. Immun.
80
483-492
2012
Escherichia coli, Escherichia coli EHEC O157:H7, Escherichia coli EPEC / E2348/69
brenda
Hui, C.Y.; Guo, Y.; He, Q.S.; Peng, L.; Wu, S.C.; Cao, H.; Huang, S.H.
Escherichia coli outer membrane protease OmpT confers resistance to urinary cationic peptides
Microbiol. Immunol.
54
452-459
2010
Escherichia coli, Escherichia coli E44
brenda
Tagai, C.; Morita, S.; Shiraishi, T.; Miyaji, K.; Iwamuro, S.
Antimicrobial properties of arginine- and lysine-rich histones and involvement of bacterial outer membrane protease T in their differential mode of actions
Peptides
32
2003-2009
2011
Escherichia coli, Escherichia coli JCM 5491
brenda
Jaervinen, H.M.; Laakkonen, L.; Haiko, J.; Johansson, T.; Juuti, K.; Suomalainen, M.; Buchrieser, C.; Kalkkinen, N.; Korhonen, T.K.
Human single-chain urokinase is activated by the omptins PgtE of Salmonella enterica and Pla of Yersinia pestis despite mutations of active site residues
Mol. Microbiol.
89
507-517
2013
Escherichia coli, Salmonella enterica, Salmonella enterica 14028R, Yersinia pestis (P17811), Yersinia pestis
brenda
da Silva, R.R.; de Oliveira, L.C.; Juliano, M.A.; Juliano, L.; de Oliveira, A.H.; Rosa, J.C.; Cabral, H.
Biochemical and milk-clotting properties and mapping of catalytic subsites of an extracellular aspartic peptidase from basidiomycete fungus Phanerochaete chrysosporium
Food Chem.
225
45-54
2017
Phanerodontia chrysosporium
brenda
Wood, S.E.; Sinsinbar, G.; Gudlur, S.; Nallani, M.; Huang, C.F.; Liedberg, B.; Mrksich, M.
A bottom-up proteomic approach to identify substrate specificity of outer-membrane protease OmpT
Angew. Chem. Int. Ed. Engl.
56
16531-16535
2017
Escherichia coli (P09169)
brenda
Hui, C.Y.; Guo, Y.; Liu, L.; Zheng, H.Q.; Wu, H.M.; Zhang, L.Z.; Zhang, W.
Development of a novel bacterial surface display system using truncated OmpT as an anchoring motif
Biotechnol. Lett.
41
763-777
2019
Escherichia coli (P09169), Escherichia coli
brenda
Riva, R.; Korhonen, T.K.; Meri, S.
The outer membrane protease PgtE of Salmonella enterica interferes with the alternative complement pathway by cleaving factors B and H
Front. Microbiol.
6
63
2015
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium 14028R
brenda
Brannon, J.R.; Burk, D.L.; Leclerc, J.M.; Thomassin, J.L.; Portt, A.; Berghuis, A.M.; Gruenheid, S.; Le Moual, H.
Inhibition of outer membrane proteases of the omptin family by aprotinin
Infect. Immun.
83
2300-2311
2015
Citrobacter rodentium, Escherichia coli (P09169), Escherichia coli
brenda
Samykannu, G.; Vijayababu, P.; Natarajan, J.
Substrate specificities in Salmonella typhi outer membrane protease (PgtE) from omptin family - an in silico proteomic approach
Inform. Med. Unlocked
12
6-13
2018
Salmonella enterica subsp. enterica serovar Typhi (Q8Z4Y4)
-
brenda
Brannon, J.R.; Thomassin, J.L.; Gruenheid, S.; Le Moual, H.
Antimicrobial peptide conformation as a structural determinant of omptin protease specificity
J. Bacteriol.
197
3583-3591
2015
Citrobacter rodentium, Escherichia coli (P58603), Escherichia coli, Citrobacter rodentium ATCC 51459, Citrobacter rodentium DBS 100, Escherichia coli EDL933 (P58603)
brenda
Korhonen, T.K.
Fibrinolytic and procoagulant activities of Yersinia pestis and Salmonella enterica
J. Thromb. Haemost.
13 Suppl 1
S115-S120
2015
Salmonella enterica subsp. enterica serovar Typhimurium (P06185), Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (P06185), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (P06185)
brenda
Feodorova, V.A.; Lyapina, A.M.; Zaitsev, S.S.; Khizhnyakova, M.A.; Sayapina, L.V.; Ulianova, O.V.; Ulyanov, S.S.; Motin, V.L.
New promising targets for synthetic omptin-based peptide vaccine against Gram-negative pathogens
Vaccines (Basel)
7
36
2019
Salmonella enterica subsp. enterica serovar Typhimurium (P06185), Escherichia coli (P09169), Escherichia coli (P34210), Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (P06185), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (P06185)
brenda
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EXTERNAL LINKS (specific for EC-Number 3.4.23.49)
Transporter Classification Database (TCDB): 9.B.50.1.1
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