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Information on EC 3.4.23.49 - omptin and Organism(s) Escherichia coli and UniProt Accession P34210
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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 taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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 protein 3b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
OmpP protease
F episome-encoded outer membrane protease, 71% amino acid sequence identity with OmpT protease
Gene ompT proteins
-
-
-
-
ompT
OmpT protease
Omptin
-
-
-
-
Outer membrane protein 3B
-
-
-
-
Pla
-
-
-
-
protease 7
Protease A
-
-
-
-
Protease VII
-
-
-
-
Protein a
-
-
-
-
Proteins, specific or class, gene ompT
-
-
-
-
additional information
-
the enzymes belong to the omptin family of enterobacterial surface proteases/adhesins
ompT
-
-
OmpT protease
-
-
-
-
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.
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-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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
150770-86-8
-
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
WEEGGRRIGRGGK + H2O
?
used as a control substrate for determination of the activity of OmpT protease
-
-
?
WLAAKKGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAARRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAARRGRG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLAASRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLARRRGAG + H2O
?
different cleavage sites between OmpP and OmpT protease determined
-
-
?
WLATRRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLRARRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLSARRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
WLSERRGAG + H2O
?
differences in substrate specificity between OmpP and OmpT proteases determined
-
-
?
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-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
-
-
?
aminobenzoyl-Ala-Arg-Arg-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
?
C18G + H2O
?
-
synthetic alpha-helical peptide, whose sequence has been optimized for maximal antibacterial activity
-
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
-
OmpT, proteolytic degradation
-
-
?
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
-
-
?
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 proenzyme plasminogen + H2O
?
-
low activity of OmpT in activation of the substrate, proteolytic cleavage
-
-
?
human single-chain urokinase + H2O
?
-
-
cleavage at the peptide bond Lys158-Ile159, the site cleaved also by the physiological activator human plasmin
-
?
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
-
-
?
L-Ala-L-Arg-L-Arg-L-Ala + H2O
L-Ala-L-Arg + L-Arg-L-Ala
-
model peptide substrate
-
-
?
LL-37 + H2O
?
-
human antimicrobial peptide of the cathelicidin family, cleavage occurs at dibasic sites
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
CRAMP
-
-
?
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 hormone13-34 + H2O
?
-
human, cleaved at both Arg25-Lys26 and Lys26-Lys27
-
-
?
plasminogen + H2O
heavy and light chain of plasmin + ?
-
cleavage at an Arg-Val bond
-
?
Protein expressed from a fusion gene + H2O
?
-
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
-
-
?
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
-
-
?
WLAAKKGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAARRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAARRGRG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLAASRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLARRRGAG + H2O
?
different cleavage sites between OmpT and OmpP protease determined
-
-
?
WLATRRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLRARRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLSARRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
WLSERRGAG + H2O
?
differences in substrate specificity between OmpT and OmpP proteases determined
-
-
?
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
-
-
?
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
-
?
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
?
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
-
-
?
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
-
-
?
T7 RNA polymerase + H2O
?
-
cleavage at Lys-Arg173, Lys-Lys180, and Arg-Lys392
-
-
?
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
-
-
?
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
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
-
OmpT, proteolytic degradation
-
-
?
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
-
-
?
human proenzyme plasminogen + H2O
?
-
low activity of OmpT in activation of the substrate, proteolytic cleavage
-
-
?
LL37 + H2O
?
a human antimicrobial peptide of the cathelicidin family
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
CRAMP
-
-
?
small-molecular-weight chromogenic peptides + H2O
?
-
OmpT, proteolytic cleavage
-
-
?
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
-
-
?
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
-
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
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lipopolysaccharide
purified OmpP protease active only in the presence of, similar to OmpT protein homologue
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
OmpT protein active only in the presence of
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
WEEGGRRIGRGGK
used as a control substrate for determination of the activity of OmpT protease
0.19
WLARRRGAG
different cleavage sites used by OmpP or OmpT proteases
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
0.0013
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
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
0.53
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.4
WEEGGRRIGRGGK
used as a control substrate for determination of the activity of OmpT protease
2.2
WLARRRGAG
different cleavage sites used by OmpP or OmpT proteases
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
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
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
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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 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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
additional information
-
proteolytic cleavage observed only under neutral conditions
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
integral membrane protease, outer membrane, membrane bound
-
dimyristoylphosphatidylcholine lipid bilayer embedded beta-barrel
-
enzyme incorporation mechanism into membranes, overview
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
malfunction
-
using gene deletions, it is demonstrated that bacterial inactivation of tissue factor pathway inhibitor (TFPI) requires omptin expression
physiological function
additional information
acidic residues in the active site are the catalytic pairs Asp83-Asp85 and His212-Asp210
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
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
Escherichia coli OmpT inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
180000
33500
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
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
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
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
-
ompT is associated in inclusion bodies and active in the presence of high concentrations
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL1-Blue, additional strains and plasmids listed, construction of phage libraries and substrate phage described
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
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
-
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)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the ompT gene is higher in EHEC strains than in EPEC strains
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
biotechnology
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
Baaden, M.; Sansom, M.S.
OmpT: molecular dynamics simulations of an outer membrane enzyme
Biophys. J.
87
2942-2953
2004
Escherichia coli
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
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
Erwinia pyrifoliae, Escherichia coli, Salmonella enterica, Shigella flexneri, Yersinia pestis
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
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
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)
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)
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)
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
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)
Duche, D.; Issouf, M.; Lloubes, R.
Immunity protein protects colicin E2 from OmpT protease
J. Biochem.
145
95-101
2009
Escherichia coli
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
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
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
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
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
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
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)
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
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
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)
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)
EXTERNAL LINKS (specific for EC-Number 3.4.23.49)
Transporter Classification Database (TCDB): 9.B.50.1.1
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