3.4.22.B19: YopJ protease
This is an abbreviated version!
For detailed information about YopJ protease, go to the full flat file.
Word Map on EC 3.4.22.B19
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3.4.22.B19
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enterocolitica
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pestis
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pseudotuberculosis
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plague
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yersinia-infected
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listeriolysin
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iii-dependent
- 3.4.22.B19
- enterocolitica
- pestis
- pseudotuberculosis
- plague
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yersinia-infected
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listeriolysin
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iii-dependent
Reaction
cleaves reversible post-translational modification in form of ubiquitin or a ubiquitin-like protein. It inhibits the host immune response and induces apoptosis by blocking multiple signaling pathways, including the MAPK and NfkappaB pathways in the infected cell =
Synonyms
C55.001, outer protein T, virulence factor YopJ, Yersinia outer protein, Yersinia outer protein J, Yersinia outer protein P, Yersinia outer protein T, YopJ, YopJKIM, YopP, YopT
ECTree
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Substrates Products
Substrates Products on EC 3.4.22.B19 - YopJ protease
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REACTION DIAGRAM
ubiquitin-7-amido-4-methylcoumarin + H2O
ubiquitin + 7-amino-4-methylcoumarin
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TRAF2 + ubiquitin
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YopJ is a promiscuous deubiquitinating enzyme that negatively regulates signaling by removing ubiquitin moieties from proteins, such as TRAF2, TRAF6, and IkappaBalpha. YopJ cleaves both K48- and K63-linked polyubiquitin
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TRAF3-ubiquitin + H2O
TRAF3 + ubiquitin
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YopJ is a deubiquitinating protease that acts on TRAF proteins to prevent or remove the K63-polymerized ubiquitin conjugates required for signal transduction
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TRAF6-ubiquitin + H2O
TRAF6 + ubiquitin
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YopJ is a deubiquitinating protease that acts on TRAF proteins to prevent or remove the K63-polymerized ubiquitin conjugates required for signal transduction
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TRAF6-ubiquitin + H2O
TRAF6 + ubiquitin
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YopJ is a promiscuous deubiquitinating enzyme that negatively regulates signaling by removing ubiquitin moieties from proteins, such as TRAF2, TRAF6, and IkappaBalpha. YopJ cleaves both K48- and K63-linked polyubiquitin
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pathogenic Yersinia spp. secrete the effector YopJ into host cells to counteract cytokine production and to induce programmed cell death. YopJ achieves these aims by inactivating mitogen-activated protein kinase and nuclear factor kappaB signaling pathways. YopJ binds to members of the MAPK kinase family and is predicted to have protease activity toward ubiquitin-like proteins
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additional information
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interaction of Yersinia pestis with macrophages, limitations in YopJ-dependent apoptosis
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additional information
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pathogenic Yersinia spp. secrete the effector YopJ into host cells to counteract cytokine production and to induce programmed cell death. YopJ achieves these aims by inactivating mitogen-activated protein kinase and nuclear factor kappaB signaling pathways. YopJ binds to members of the MAPK kinase family and is predicted to have protease activity toward ubiquitin-like proteins
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additional information
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mice infected with wild-type strain of Yersinia pseudotuberculosis show the highest TNF-alpha production on the 21st day after infection in the culture supernatant of cells incubated with LPS. During the infection with mutant strains unable to secrete YopJ, there is no TNF-alpha production on both the 7th and 28th days after infection, but the production is increased on the 21st day with the cells incubated with LPS and HKY (2.1fold higher than the control group)
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additional information
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pathogenic Yersinia spp. secrete the effector YopJ into host cells to counteract cytokine production and to induce programmed cell death. YopJ achieves these aims by inactivating mitogen-activated protein kinase and nuclear factor kappaB signaling pathways. YopJ binds to members of the MAPK kinase family and is predicted to have protease activity toward ubiquitin-like proteins
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additional information
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no cleavage of (SUMO-1)-7-amido-4-methylcoumarin
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additional information
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the virulence factor YopJ cleaves reversibly post-translational modification in form of ubiquitin or a ubiquitin-like protein. It inhibits the host immune response and induces apoptosis by blocking multiple signaling pathways, including the MAPK and NfkappaB pathways in the infected cell
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additional information
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substrates are highly conserved ubiquitin-like molecules, which are covalently added to numerous regulatory proteins. YopJ protease exerts its pathogenic effect on cells by disrupting this posttranslational modification
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additional information
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YopJ is delivered into the target host cytosol via a type III secretion system. YopJ blocks activation of the superfamily of MAPK kinases, including MKKs and IKKbeta. The inhibition results in the inability of the cell to produce cytokines and antiapoptotic machinery
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additional information
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YopJ uses acetyl-coenzyme A to modify the critical serine and threonine residues in the activation loop of MAPKK6 and thereby blocking phosphorylation
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