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2-aminobenzoyl-AKKA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
2-aminobenzoyl-AKRA-3-[(2,4-dinitrophenyl)amino]-L-alanyl-Gly + H2O
?
-
-
-
?
2-aminobenzoyl-ARKA-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
-
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
Abz-SLGR + KIQIK(Dnp)-NH2
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
-
-
?
acetyl-Ala-Lys-(D)Arg-Val-Gly-(beta)-Ala + H2O
?
-
-
-
?
alpha-Neo-endorphin + H2O
?
-
cleaved at Arg6-Lys7
-
-
?
alpha-neoendorphin + H2O
?
-
proteolytic cleavage site GFLR*KYPK
-
-
?
alpha2-antiplasmin + H2O
?
ALYKKLLKKLLKSAKKLG + H2O
?
synthetic alpha-antimicrobial peptide L-C18G, D-amino acids are not degraded by CroP
-
-
?
aminobenzoyl-Ala-Arg-Arg-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
-
-
-
?
aminobenzoyl-Ala-Lys-Lys-Ala-3-(dinitrophenyl)diaminopropionic acid-Gly + H2O
?
aminobenzoyl-ARRA-Tyr(NO2)-G + H2O
?
-
-
-
?
calf thymus histone H2B + H2o
?
calf thymus histone H3 + H2o
?
calf thymus histone H4 + H2o
?
cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP, a murine cathelicidin-related antimicrobial peptide
-
-
?
cationic antimicrobial peptides from epithelial cells or macrophages + H2O
?
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
-
-
?
dynorphin A(1-13) + H2O
Tyr-Gly-Gly-Phe-Leu-Arg + Arg-Ile-Arg-Pro-Lys-Leu-Lys
-
proteolytic cleavage site GFLR*RIRPK
-
-
?
ELELYKRHHG + H2O
ELELYK + RHHG
-
-
-
?
ELRLYKAHHGSG + H2O
ELRLYK + AHHGSG
-
-
-
?
ELRLYKKHHGSG + H2O
ELRLYK + KHHGSG
-
-
-
?
ELRLYKRHHG + H2O
ELRLYK + RHHG
ELRLYKRHHGSG + H2O
ELRLYK + RHHGSG
-
-
-
?
ELRLYKSHHGSG + H2O
ELRLYK + SHHGSG
-
-
-
?
ELRLYRAHHGSG + H2O
ELRLYR + AHHGSG
-
-
-
?
ELRLYRCHHGSG + H2O
ELRLYR + CHHGSG
-
-
-
?
ELRLYRFHHGSG + H2O
ELRLYR + FHHGSG
-
-
-
?
ELRLYRIHHGSG + H2O
ELRLYR + IHHGSG
-
-
-
?
ELRLYRKHHGSG + H2O
ELRLYR + KHHGSG
-
-
-
?
ELRLYRLHHGSG + H2O
ELRLYR + LHHGSG
-
-
-
?
ELRLYRMHHGSG + H2O
ELRLYR + MHHGSG
-
-
-
?
ELRLYRNHHG + H2O
ELRLYR + NHHG
-
-
-
?
ELRLYRNHHGSG + H2O
ELR + LYR + NHHGSG
-
-
-
?
ELRLYRPHHGSG + H2O
ELR + LYRPHHGSG
-
-
-
?
ELRLYRQHHGSG + H2O
ELRLYR + QHHGSG
-
-
-
?
ELRLYRRHHG + H2O
ELRLYR + RHHG
-
-
-
?
ELRLYRRHHGSG + H2O
ELRLYR + RHHGSG
-
-
-
?
ELRLYRSHHGSG + H2O
ELRLYR + SHHGSG
-
-
-
?
ELRLYRTHHGSG + H2O
ELRLYR + THHGSG
-
-
-
?
ELRLYRVHHGSG + H2O
ELRLYR + VHHGSG
-
-
-
?
ELRLYRWHHGSG + H2O
ELR + LYR + WHHGSG
-
-
-
?
ELRLYRYHHGSG + H2O
ELR + LYR + YHHGSG
-
-
-
?
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 antiprotease alpha2-antiplasmin + H2O
?
human calcitonin precursor + H2O
?
-
proteolytic cleavage by mutant D97H at an N-terminal Cys
-
-
?
human circulating complement proteins + H2O
?
human creatin kinase + H2O
?
-
proteolytic cleavage site DIYK*KLRDK
-
-
?
human plasminogen + H2O
?
-
proteolytic cleavage site CPGR*VVGGC, activation
-
-
?
human proenzyme plasminogen + H2O
?
human single-chain urokinase + H2O
?
human tissue factor pathway inhibitor + H2O
?
IAA-Arg-Arg-p-nitroanilide + H2O
?
-
-
-
?
Inclusion bodies from E. coli solubilized by denaturation + H2O
?
-
-
-
-
?
L-Ala-L-Arg-L-Arg-L-Ala + H2O
L-Ala-L-Arg + L-Arg-L-Ala
-
model peptide substrate
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
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
-
-
?
o-aminobenzoyl-Ala-Arg-Arg-Ala-3-nitrotyrosine-NH2 + H2O
?
-
-
-
?
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
-
-
?
PAI-1 + H2O
?
-
a serpin
-
-
?
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 + H2O
plasmin + ?
plasminogen activator inhibitor-1 + H2O
?
inactivation
-
-
?
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
-
-
?
rabbit creatine kinase + H2O
?
-
proteolytic cleavage sites DLYK*KLRDK and RGER*RAVEK
-
-
?
Rabbit muscle creatine kinase + H2O
?
-
-
-
-
?
Recombinant human gamma-interferon + H2O
?
-
cleavage between basic amino acids
-
-
?
RLELYKRHHG + H2O
RLELYK + RHHG
-
-
-
?
RLRLYKRHHG + H2O
RLRLYK + RHHG
-
-
-
?
RRELRLYRRHHG + H2O
?
-
-
-
-
?
RRLELYKRHHG + H2O
?
-
-
-
-
?
RSANP + H2O
ANP + ?
-
atrial natriuretic peptide
-
?
RSANPR + H2O
ANP + ?
-
atrial natriuretic peptide
-
?
small-molecular-weight chromogenic peptides + H2O
?
-
OmpT, proteolytic cleavage
-
-
?
T7 RNA polymerase + H2O
?
tissue factor pathway inhibitor + H2O
?
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
-
-
?
additional information
?
-
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
-
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
-
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
Abz-SLGR + KIQIK(Dnp)-NH2
-
-
-
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
Abz-SLGR + KIQIK(Dnp)-NH2
-
-
-
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
Abz-SLGR + KIQIK(Dnp)-NH2
-
-
-
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
Abz-SLGR + KIQIK(Dnp)-NH2
-
-
-
?
Abz-SLGRKIQIK(Dnp)-NH2 + H2O
Abz-SLGR + KIQIK(Dnp)-NH2
-
-
-
?
alpha2-antiplasmin + H2O
?
-
a serpin
-
-
?
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
?
-
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 H2B + H2o
?
-
-
strong fragmentation of histone H2B
-
?
calf thymus histone H3 + H2o
?
-
-
moderate fragmentation of histone H3
-
?
calf thymus histone H3 + H2o
?
-
-
moderate fragmentation of histone H3
-
?
calf thymus histone H4 + H2o
?
-
-
slight fragmentation of histone H4
-
?
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
?
-
-
-
?
dynorphin A + H2O
?
-
-
-
?
dynorphin A + H2O
?
-
cleavage at Arg6-Arg7
-
-
?
dynorphin A + H2O
?
-
proteolytic cleavage, commercial peptide substrate
-
-
?
dynorphin A + H2O
?
cleavage assay of OmpT protease performed with
-
-
?
ELRLYKRHHG + H2O
ELRLYK + RHHG
-
-
-
?
ELRLYKRHHG + H2O
ELRLYK + RHHG
-
-
-
?
factor B + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
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 + H2O
?
-
factor H is cleaved at both N- and C-termini, while the central region resists proteolysis
-
-
?
factor H + H2O
?
-
-
-
-
?
factor H + H2O
?
-
factor H is cleaved at both N- and C-termini, while the central region resists proteolysis
-
-
?
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 LL-37 + H2O
?
-
a cathelicidin
-
-
?
human LL-37 + H2O
?
-
a cathelicidin
-
-
?
human LL-37 + H2O
?
-
a cathelicidin
-
-
?
human LL-37 + H2O
?
a cathelicidin
-
-
?
human LL-37 + H2O
?
a cathelicidin
-
-
?
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
?
-
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
-
-
?
Mastoparan + H2O
?
-
cleavage at Lys11-Lys12
-
-
?
Mastoparan + H2O
?
-
proteolytic cleavage site ALAK*KIL
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP, rapid, almost complete degradation
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP, rapid, almost complete degradation
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
-
CRAMP, rapid, almost complete degradation
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
CRAMP
-
-
?
murine cathelicidin-related antimicrobial peptide + H2O
?
CRAMP
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
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
-
-
?
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
?
-
-
-
-
?
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 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 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
?
-
-
preference for denatured substrates
-
-
?
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
?
-
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
?
-
-
substrate specificity analysis
-
-
?
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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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
the enzyme belongs to the omptin family of enzymes
evolution
-
the enzyme belongs to the omptin family of enzymes
evolution
-
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
-
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
-
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 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
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physiological function
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OmpT is involved in the antimicrobial properties of Arg- and Lys-rich histones and the modes of antimicrobial action of these histones are different
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physiological function
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Citrobacter rodentium inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively. CroP preferentially cleaves unstructured antimicrobial peptides (AMPs)
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physiological function
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deletion mutant is more susceptible to alpha-helical antimicrobial peptides
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physiological function
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Escherichia coli OmpT inactivates antimicrobial peptides (AMPs) and activates plasminogen into plasmin, respectively
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physiological function
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deletion mutant is more susceptible to alpha-helical antimicrobial peptides
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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
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D210A
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site-directed mutagenesis by overlap extension PCR
H212A
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site-directed mutagenesis by overlap extension PCR
D208A
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introduced as silent mutation in plasmids, transformation with plasmids
D208G
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site-directed mutagenesis, the mutant enzyme shows increased specificity for the A-R cleavage site compared to the wild-type enzyme
D210A
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introduced as silent mutation in plasmids, transformation with plasmids
D43A
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introduced as silent mutation in plasmids, transformation with plasmids
D83A
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introduced as silent mutation in plasmids, transformation with plasmids
D85A
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introduced as silent mutation in plasmids, transformation with plasmids
D97C
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97F
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97H
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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
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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
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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
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97Q
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97S
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
D97T
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
E111A
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introduced as silent mutation in plasmids, transformation with plasmids
E136A
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introduced as silent mutation in plasmids, transformation with plasmids
E193A
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introduced as silent mutation in plasmids, transformation with plasmids
E250A
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introduced as silent mutation in plasmids, transformation with plasmids
E27A
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introduced as silent mutation in plasmids, transformation with plasmids
H212A
molecular mechanics/coarse-grained (MM/CG) simulation applied
S223R
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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
molecular mechanics/coarse-grained (MM/CG) simulation applied
S99A/G216K/K217G
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recombinant ompT variant in order to abolish autoproteolysis
D97A
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introduced as silent mutation in plasmids, transformation with plasmids
D97A
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site-directed mutagenesis, mutant shows altered cleavage specificity compared to the wild-type enzyme, substrate specificity with fusion protein, overview
G216K/K217G
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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
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site-directed mutagenesis, inacticve catalytic site mutant
D206A
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site-directed mutagenesis, inacticve catalytic site mutant
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additional information
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generation of a Citrobacter rodentium DELTAcroP strain
additional information
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generation of a deletion mutant DELTAcroP
additional information
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generation of a deletion mutant DELTAcroP
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additional information
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generation of a deletion mutant DELTAcroP
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additional information
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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
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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
generation of a deletion mutant DELTAompT
additional information
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generation of a deletion mutant DELTAompT
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
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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
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generation of a deletion mutant DELTAompT
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additional information
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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
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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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Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues: identity of protease VII and OmpT
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A novel activity of OmpT. Proteolysis under extreme denaturing conditions
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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
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Substrate specificity of the integral membrane protease ompT determined by spatially addressed peptide libraries
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Artifactual cleavage of E. coli H-NS by OmpT
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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
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66
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2002
Escherichia coli, no activity in Escherichia coli, no activity in Escherichia coli W3110 / ATCC 27325
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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
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Escherichia coli, no activity in Escherichia coli, no activity in Escherichia coli W3110 / ATCC 27325
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Utilization of Escherichia coli outer-membrane endoprotease OmpT variants as processing enzymes for production of peptides from designer fusion proteins
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OmpT: molecular dynamics simulations of an outer membrane enzyme
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Escherichia coli
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The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis
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Escherichia coli, Salmonella enterica, Yersinia pestis, Shigella flexneri, Erwinia pyrifoliae
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Substrate specificity of the Escherichia coli outer membrane protease OmpT
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Escherichia coli K-12
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Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity
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Escherichia coli (P09169), Escherichia coli
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Role of the ompT mutation in stimulated decrease in colony-forming ability due to intracellular protein aggregate formation in Escherichia coli strain BL21
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Escherichia coli (P09169)
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Modulation of infectivity in phage display as a tool to determine the substrate specificity of proteases
Chembiochem
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Initial steps of colicin E1 import across the outer membrane of Escherichia coli
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Substrate specificity of the Escherichia coli outer membrane protease OmpP
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Identification and antibody-therapeutic targeting of chloramphenicol-resistant outer membrane proteins in Escherichia coli
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Immunity protein protects colicin E2 from OmpT protease
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Size and dynamics of the Vibrio cholerae porins OmpU and OmpT probed by polymer exclusion
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Proteolytic inactivation of tissue factor pathway inhibitor by bacterial omptins
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Escherichia coli, Salmonella enterica
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The bactericidal action on Escherichia coli of ZF-RNase-3 is triggered by the suicidal action of the bacterium OmpT protease
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Escherichia coli DH5[alpha], Escherichia coli DH5-alpha
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Enhanced fluorescent properties of an OmpT site deleted mutant of green fluorescent protein
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Escherichia coli
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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
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Escherichia coli, Escherichia coli E44
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Wood, S.E.; Sinsinbar, G.; Gudlur, S.; Nallani, M.; Huang, C.F.; Liedberg, B.; Mrksich, M.
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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
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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
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Brannon, J.R.; Burk, D.L.; Leclerc, J.M.; Thomassin, J.L.; Portt, A.; Berghuis, A.M.; Gruenheid, S.; Le Moual, H.
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Samykannu, G.; Vijayababu, P.; Natarajan, J.
Substrate specificities in Salmonella typhi outer membrane protease (PgtE) from omptin family - an in silico proteomic approach
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Salmonella enterica subsp. enterica serovar Typhi (Q8Z4Y4)
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Brannon, J.R.; Thomassin, J.L.; Gruenheid, S.; Le Moual, H.
Antimicrobial peptide conformation as a structural determinant of omptin protease specificity
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Fibrinolytic and procoagulant activities of Yersinia pestis and Salmonella enterica
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Salmonella enterica subsp. enterica serovar Typhimurium (P06185), Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (P06185), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (P06185)
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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