YOPJ_YERPS
ID YOPJ_YERPS Reviewed; 288 AA.
AC P0DUC9; 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 7.
DE RecName: Full=Serine/threonine-protein acetyltransferase YopJ {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:A0A0N9NCU6};
DE AltName: Full=Virulence factor YopJ;
GN Name=yopJ {ECO:0000250|UniProtKB:A0A0N9NCU6}; OrderedLocusNames=pYV0098;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OG Plasmid pYV.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953; PLASMID=pYV;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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. Inhibits the
CC MAPK and NF-kappa-B signaling pathways by acetylating protein-kinases
CC such as MAP2K1, MAP2K6, MAP3K7/TAK1 and I-kappa-B kinase (CHUK/IKKA and
CC IKBKB) on serine and threonine residues critical for their activation
CC by phosphorylation, thereby preventing protein-kinase activation.
CC Promotes pyroptosis, a programmed cell death, in host cells by
CC mediating acetylation of MAP3K7/TAK1: MAP3K7/TAK1 inactivation triggers
CC activation of caspase-8 (CASP8), followed by CASP8-dependent cleavage
CC of gasdermin-D (GSDMD) and induction of pyroptosis (By similarity).
CC Also able to induce intestinal barrier dysfunction by acetylating and
CC inhibiting host protein-kinases RIPK2/RICK and MAP3K7/TAK1, thereby
CC promoting cell death (By similarity).
CC {ECO:0000250|UniProtKB:A0A0N9NCU6, ECO:0000250|UniProtKB:P0DUD0}.
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:0000250|UniProtKB:A0A0N9NCU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65341;
CC Evidence={ECO:0000250|UniProtKB:A0A0N9NCU6};
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:0000250|UniProtKB:A0A0N9NCU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393;
CC Evidence={ECO:0000250|UniProtKB:A0A0N9NCU6};
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:0000250|UniProtKB:P0DUD0}.
CC Note=Secreted via type III secretion system (TTSS).
CC {ECO:0000250|UniProtKB:P0DUD0}.
CC -!- SIMILARITY: Belongs to the acetyltransferase YopJ family.
CC {ECO:0000305}.
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DR EMBL; BX936399; CAF25441.1; -; Genomic_DNA.
DR RefSeq; WP_002225474.1; NZ_CP009711.1.
DR AlphaFoldDB; P0DUC9; -.
DR SMR; P0DUC9; -.
DR DIP; DIP-61317N; -.
DR IntAct; P0DUC9; 1.
DR GeneID; 66841083; -.
DR KEGG; ypo:BZ17_4238; -.
DR KEGG; yps:pYV0098; -.
DR OMA; FAMAEMD; -.
DR Proteomes; UP000001011; Plasmid pYV.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR005083; Ser/Thr_AcTrfase.
DR Pfam; PF03421; Acetyltransf_14; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Allosteric enzyme; Plasmid; Secreted; Transferase;
KW Virulence.
FT CHAIN 1..288
FT /note="Serine/threonine-protein acetyltransferase YopJ"
FT /id="PRO_0000451625"
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:0000250|UniProtKB:Q6VE93"
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"
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
