YOPJ_YERPY
ID YOPJ_YERPY Reviewed; 288 AA.
AC P0DUD0; P31498; Q663G8; Q6J1F6;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=Serine/threonine-protein acetyltransferase YopJ {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:22520462};
DE AltName: Full=Virulence factor YopJ {ECO:0000305};
GN Name=yopJ {ECO:0000303|PubMed:8045884}; OrderedLocusNames=pYV0098;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OG Plasmid pIB1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RC STRAIN=YPIII / Serotype O:3; PLASMID=pIB1;
RX PubMed=8045884; DOI=10.1128/jb.176.15.4543-4548.1994;
RA Galyov E.E., Haakansson S., Wolf-Watz H.;
RT "Characterization of the operon encoding the YpkA Ser/Thr protein kinase
RT and the YopJ protein of Yersinia pseudotuberculosis.";
RL J. Bacteriol. 176:4543-4548(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YPIII / Serotype O:3;
RA Orth K., Palmer L.E., Bao Z.Q., Stewart S., Rudolph A.E., Bliska J.B.,
RA Dixon J.E.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-264.
RC PLASMID=pIB1;
RX PubMed=1840573; DOI=10.1128/iai.59.5.1860-1863.1991;
RA Krause M., Harwood J., Fierer J., Guiney D.;
RT "Genetic analysis of homology between the virulence plasmids of Salmonella
RT dublin and Yersinia pseudotuberculosis.";
RL Infect. Immun. 59:1860-1863(1991).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=YPIII / Serotype O:3;
RX PubMed=9535085; DOI=10.1046/j.1365-2958.1998.00740.x;
RA Palmer L.E., Hobbie S., Galan J.E., Bliska J.B.;
RT "YopJ of Yersinia pseudotuberculosis is required for the inhibition of
RT macrophage TNF-alpha production and downregulation of the MAP kinases p38
RT and JNK.";
RL Mol. Microbiol. 27:953-965(1998).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-172.
RC STRAIN=YPIII / Serotype O:3;
RX PubMed=22520462; DOI=10.1016/j.chom.2012.02.009;
RA Meinzer U., Barreau F., Esmiol-Welterlin S., Jung C., Villard C., Leger T.,
RA Ben-Mkaddem S., Berrebi D., Dussaillant M., Alnabhani Z., Roy M.,
RA Bonacorsi S., Wolf-Watz H., Perroy J., Ollendorff V., Hugot J.P.;
RT "Yersinia pseudotuberculosis effector YopJ subverts the Nod2/RICK/TAK1
RT pathway and activates caspase-1 to induce intestinal barrier dysfunction.";
RL Cell Host Microbe 11:337-351(2012).
CC -!- FUNCTION: Serine/threonine-protein acetyltransferase translocated into
CC infected cells, which inhibits the host immune response and induces
CC cell death by mediating acetylation of target proteins (PubMed:9535085,
CC PubMed:22520462). Inhibits the MAPK and NF-kappa-B signaling pathways
CC by acetylating protein-kinases such as MAP2K1, MAP2K6, MAP3K7/TAK1 and
CC I-kappa-B kinase (CHUK/IKKA and IKBKB) on serine and threonine residues
CC critical for their activation by phosphorylation, thereby preventing
CC protein-kinase activation (By similarity). Promotes pyroptosis, a
CC programmed cell death, in host cells by mediating acetylation of
CC MAP3K7/TAK1: MAP3K7/TAK1 inactivation triggers activation of caspase-8
CC (CASP8), followed by CASP8-dependent cleavage of gasdermin-D (GSDMD)
CC and induction of pyroptosis (By similarity). Also able to induce
CC intestinal barrier dysfunction by acetylating and inhibiting host
CC protein-kinases RIPK2/RICK and MAP3K7/TAK1, thereby promoting cell
CC death (PubMed:22520462). {ECO:0000250|UniProtKB:A0A0N9NCU6,
CC ECO:0000269|PubMed:22520462, ECO:0000269|PubMed:9535085}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-threonyl-[protein] = CoA + O-acetyl-L-threonyl-
CC [protein]; Xref=Rhea:RHEA:65340, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:16780, ChEBI:CHEBI:30013, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:141025; Evidence={ECO:0000269|PubMed:22520462};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65341;
CC Evidence={ECO:0000269|PubMed:22520462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-seryl-[protein] = CoA + O-acetyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:59392, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:15352, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:141128; Evidence={ECO:0000269|PubMed:22520462};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393;
CC Evidence={ECO:0000269|PubMed:22520462};
CC -!- COFACTOR:
CC Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130;
CC Evidence={ECO:0000250|UniProtKB:O68718};
CC -!- ACTIVITY REGULATION: 1D-myo-inositol hexakisphosphate activates
CC protein-acetyltransferase activity via an allosteric mechanism: 1D-myo-
CC inositol hexakisphosphate-binding induces a conformational
CC rearrangement that stimulates the interaction with acetyl-CoA.
CC {ECO:0000250|UniProtKB:Q6VE93}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8045884,
CC ECO:0000269|PubMed:9535085}. Note=Secreted via type III secretion
CC system (TTSS). {ECO:0000269|PubMed:9535085}.
CC -!- INDUCTION: At 37 degrees Celsius in the absence of calcium.
CC {ECO:0000269|PubMed:8045884}.
CC -!- SIMILARITY: Belongs to the acetyltransferase YopJ family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA27659.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA68488.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L33833; AAA68488.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY606230; AAT28340.1; -; Genomic_DNA.
DR EMBL; M58506; AAA27659.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; P0DUD0; -.
DR SMR; P0DUD0; -.
DR DIP; DIP-61317N; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016413; F:O-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0030919; P:peptidyl-serine O-acetylation; IDA:UniProtKB.
DR GO; GO:0120258; P:peptidyl-threonine O-acetylation; IDA:UniProtKB.
DR GO; GO:0052042; P:positive regulation by symbiont of host programmed cell death; IDA:UniProtKB.
DR GO; GO:0070432; P:regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IDA:UniProtKB.
DR InterPro; IPR005083; Ser/Thr_AcTrfase.
DR Pfam; PF03421; Acetyltransf_14; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Allosteric enzyme; Direct protein sequencing; Plasmid;
KW Secreted; Transferase; Virulence.
FT CHAIN 1..288
FT /note="Serine/threonine-protein acetyltransferase YopJ"
FT /id="PRO_0000066368"
FT ACT_SITE 109
FT /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT ACT_SITE 128
FT /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT ACT_SITE 172
FT /evidence="ECO:0000305|PubMed:22520462"
FT BINDING 109
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT BINDING 167..168
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT BINDING 182..185
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT BINDING 224..225
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT BINDING 227..230
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT BINDING 257
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT BINDING 266..270
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q6VE93"
FT MUTAGEN 172
FT /note="C->A: Abolished acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:22520462"
SQ SEQUENCE 288 AA; 32487 MW; 6CEC20F2A61C5010 CRC64;
MIGPISQINI SGGLSEKETS SLISNEELKN IITQLETDIS DGSWFHKNYS RMDVEVMPAL
VIQANNKYPE MNLNLVTSPL DLSIEIKNVI ENGVRSSRFI INMGEGGIHF SVIDYKHING
KTSLILFEPA NFNSMGPAML AIRTKTAIER YQLPDCHFSM VEMDIQRSSS ECGIFSFALA
KKLYIERDSL LKIHEDNIKG ILSDGENPLP HDKLDPYLPV TFYKHTQGKK RLNEYLNTNP
QGVGTVVNKK NETIVNRFDN NKSIVDGKEL SVSVHKKRIA EYKTLLKV
