| IED ID | IndEnz0002012687 |
| Enzyme Type ID | protease012687 |
| Protein Name |
Serine/threonine-protein acetyltransferase YopJ EC 2.3.1.- Virulence factor YopJ |
| Gene Name | yopJ EGX47_00330 EGX52_00040 |
| Organism | Yersinia pseudotuberculosis |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Yersiniaceae Yersinia Yersinia pseudotuberculosis complex Yersinia pseudotuberculosis |
| Enzyme Sequence | MIGPISQINISGGLSEKETSSLISNEELKNIITQLETDISDGSWFHKNYSRMDVEVMPALVIQANNKYPEMNLNLVTSPLDLSIEIKNVIENGVRSSRFIINMGEGGIHFSVIDYKHINGKTSLILFEPANFNSMGPAMLAIRTKTAIERYQLPDCHFSMVEMDIQRSSSECGIFSFALAKKLYIERDSLLKIHEDNIKGILSDGENPLPHDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQGVGTVVNKKNETIVNRFDNNKSIVDGKELSVSVHKKRIAEYKTLLKV |
| Enzyme Length | 288 |
| Uniprot Accession Number | A0A0N9NCU6 |
| Absorption | |
| Active Site | ACT_SITE 109; /evidence="ECO:0000305|PubMed:11090361"; ACT_SITE 128; /evidence="ECO:0000250|UniProtKB:Q6VE93"; ACT_SITE 172; /evidence="ECO:0000305|PubMed:11090361, ECO:0000305|PubMed:16728640" |
| Activity Regulation | ACTIVITY REGULATION: 1D-myo-inositol hexakisphosphate activates protein-acetyltransferase activity via an allosteric mechanism: 1D-myo-inositol hexakisphosphate-binding induces a conformational rearrangement that stimulates the interaction with acetyl-CoA. {ECO:0000250|UniProtKB:Q6VE93}. |
| Binding Site | BINDING 109; /note=Coenzyme A; /evidence=ECO:0000250|UniProtKB:Q6VE93; BINDING 257; /note=1D-myo-inositol hexakisphosphate; /evidence=ECO:0000250|UniProtKB:Q6VE93 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-threonyl-[protein] = CoA + O-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:65340, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:16780, ChEBI:CHEBI:30013, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:141025; Evidence={ECO:0000269|PubMed:16728640};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65341; Evidence={ECO:0000269|PubMed:16728640}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-seryl-[protein] = CoA + O-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:59392, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15352, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:141128; Evidence={ECO:0000269|PubMed:16728640};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393; Evidence={ECO:0000269|PubMed:16728640}; |
| DNA Binding | |
| EC Number | 2.3.1.- |
| Enzyme Function | FUNCTION: Serine/threonine-protein acetyltransferase translocated into infected cells, which inhibits the host immune response and induces cell death by mediating acetylation of target proteins (PubMed:10489373, PubMed:12433923, PubMed:16728640, PubMed:22563435, PubMed:26810037). Inhibits the MAPK and NF-kappa-B signaling pathways by acetylating protein-kinases such as MAP2K1, MAP2K6, MAP3K7/TAK1 and I-kappa-B kinase (CHUK/IKKA and IKBKB) on serine and threonine residues critical for their activation by phosphorylation, thereby preventing protein-kinase activation (PubMed:16728640, Ref.9, PubMed:30361383). Promotes pyroptosis, a programmed cell death, in host cells by mediating acetylation of MAP3K7/TAK1: MAP3K7/TAK1 inactivation triggers activation of caspase-8 (CASP8), followed by CASP8-dependent cleavage of gasdermin-D (GSDMD) and induction of pyroptosis (PubMed:30381458, PubMed:30361383). Also able to induce intestinal barrier dysfunction by acetylating and inhibiting host protein-kinases RIPK2/RICK and MAP3K7/TAK1, thereby promoting cell death (By similarity). {ECO:0000250|UniProtKB:P0DUD0, ECO:0000269|PubMed:10489373, ECO:0000269|PubMed:12433923, ECO:0000269|PubMed:16728640, ECO:0000269|PubMed:22563435, ECO:0000269|PubMed:26810037, ECO:0000269|PubMed:30361383, ECO:0000269|PubMed:30381458, ECO:0000269|Ref.9}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (2); Chain (1); Mutagenesis (2); Region (5) |
| Keywords | Acyltransferase;Allosteric enzyme;Plasmid;Secreted;Transferase;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DUD0}. Note=Secreted via type III secretion system (TTSS). {ECO:0000250|UniProtKB:P0DUD0}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | Plasmid pYV2666 |
| Mass | 32,487 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:65340; RHEA:65341; RHEA:59392; RHEA:59393 |
| Cross Reference Brenda |