YOPJ_YERPE
ID YOPJ_YERPE Reviewed; 288 AA.
AC O68718; A0A6B3T9G8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Serine/threonine-protein acetyltransferase YopJ {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:22802624};
DE AltName: Full=Virulence factor YopJ {ECO:0000305};
GN Name=yopJ {ECO:0000303|PubMed:20430892};
GN Synonyms=Y0010 {ECO:0000303|PubMed:9748454},
GN yopP {ECO:0000303|PubMed:9746557};
OS Yersinia pestis.
OG Plasmid pCD1 {ECO:0000312|EMBL:AAC62603.1}.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=9746557; DOI=10.1128/iai.66.10.4611-4623.1998;
RA Perry R.D., Straley S.C., Fetherston J.D., Rose D.J., Gregor J.,
RA Blattner F.R.;
RT "DNA sequencing and analysis of the low-Ca2+-response plasmid pCD1 of
RT Yersinia pestis KIM5.";
RL Infect. Immun. 66:4611-4623(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=9748454; DOI=10.1128/jb.180.19.5192-5202.1998;
RA Hu P., Elliott J., McCready P., Skowronski E., Garnes J., Kobayashi A.,
RA Brubaker R.R., Garcia E.;
RT "Structural organization of virulence-associated plasmids of Yersinia
RT pestis.";
RL J. Bacteriol. 180:5192-5202(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=31;
RA Balykova A., Alhova Z., Eroshenko G., Kukleva L., Chervyakova N.,
RA Kyturev V.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=578;
RA Eroshenko G., Alhova Z.A., Balykova A., Kukleva L., Chervyakova N.,
RA Krasnov Y., Kyturev V.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, COFACTOR, ACTIVE SITE, AND MUTAGENESIS OF CYS-172.
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=20430892; DOI=10.1074/jbc.m110.126581;
RA Mittal R., Peak-Chew S.Y., Sade R.S., Vallis Y., McMahon H.T.;
RT "The acetyltransferase activity of the bacterial toxin YopJ of Yersinia is
RT activated by eukaryotic host cell inositol hexakisphosphate.";
RL J. Biol. Chem. 285:19927-19934(2010).
RN [6]
RP FUNCTION.
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=22563435; DOI=10.1371/journal.pone.0036019;
RA Zheng Y., Lilo S., Mena P., Bliska J.B.;
RT "YopJ-induced caspase-1 activation in Yersinia-infected macrophages:
RT independent of apoptosis, linked to necrosis, dispensable for innate host
RT defense.";
RL PLoS ONE 7:e36019-e36019(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-172.
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=22802624; DOI=10.1073/pnas.1008203109;
RA Paquette N., Conlon J., Sweet C., Rus F., Wilson L., Pereira A.,
RA Rosadini C.V., Goutagny N., Weber A.N., Lane W.S., Shaffer S.A.,
RA Maniatis S., Fitzgerald K.A., Stuart L., Silverman N.;
RT "Serine/threonine acetylation of TGFbeta-activated kinase (TAK1) by
RT Yersinia pestis YopJ inhibits innate immune signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12710-12715(2012).
RN [8]
RP FUNCTION.
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=26810037; DOI=10.1128/iai.00843-15;
RA Schoberle T.J., Chung L.K., McPhee J.B., Bogin B., Bliska J.B.;
RT "Uncovering an Important Role for YopJ in the Inhibition of Caspase-1 in
RT Activated Macrophages and Promoting Yersinia pseudotuberculosis
RT Virulence.";
RL Infect. Immun. 84:1062-1072(2016).
RN [9]
RP FUNCTION.
RX PubMed=30381458; DOI=10.1073/pnas.1809548115;
RA Sarhan J., Liu B.C., Muendlein H.I., Li P., Nilson R., Tang A.Y.,
RA Rongvaux A., Bunnell S.C., Shao F., Green D.R., Poltorak A.;
RT "Caspase-8 induces cleavage of gasdermin D to elicit pyroptosis during
RT Yersinia infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E10888-E10897(2018).
RN [10]
RP FUNCTION.
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=30361383; DOI=10.1126/science.aau2818;
RA Orning P., Weng D., Starheim K., Ratner D., Best Z., Lee B., Brooks A.,
RA Xia S., Wu H., Kelliher M.A., Berger S.B., Gough P.J., Bertin J.,
RA Proulx M.M., Goguen J.D., Kayagaki N., Fitzgerald K.A., Lien E.;
RT "Pathogen blockade of TAK1 triggers caspase-8-dependent cleavage of
RT gasdermin D and cell death.";
RL Science 362:1064-1069(2018).
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
CC (PubMed:20430892, PubMed:22563435, PubMed:22802624, PubMed:26810037).
CC Inhibits the MAPK and NF-kappa-B signaling pathways by acetylating
CC protein-kinases such as MAP2K1, MAP2K6, MAP3K7/TAK1 and I-kappa-B
CC kinase (CHUK/IKKA and IKBKB) on serine and threonine residues critical
CC for their activation by phosphorylation, thereby preventing protein-
CC kinase activation (PubMed:20430892, PubMed:22802624). Promotes
CC pyroptosis, a programmed cell death, in host cells by mediating
CC 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 (PubMed:30381458,
CC PubMed:30361383). {ECO:0000269|PubMed:20430892,
CC ECO:0000269|PubMed:22563435, ECO:0000269|PubMed:22802624,
CC ECO:0000269|PubMed:26810037, ECO:0000269|PubMed:30361383,
CC ECO:0000269|PubMed:30381458}.
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:22802624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65341;
CC Evidence={ECO:0000269|PubMed:22802624};
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:22802624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393;
CC Evidence={ECO:0000269|PubMed:22802624};
CC -!- COFACTOR:
CC Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130;
CC Evidence={ECO:0000269|PubMed:20430892};
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}.
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; AF053946; AAC62603.1; -; Genomic_DNA.
DR EMBL; AF074612; AAC69766.1; -; Genomic_DNA.
DR EMBL; JAAIKW010000129; NEX98940.1; -; Genomic_DNA.
DR EMBL; JAAIKY010000170; NEY10904.1; -; Genomic_DNA.
DR PIR; T43620; T43620.
DR RefSeq; NP_857777.1; NC_004836.1.
DR RefSeq; NP_857908.1; NC_004839.1.
DR RefSeq; WP_002224250.1; NZ_WUCM01000117.1.
DR AlphaFoldDB; O68718; -.
DR SMR; O68718; -.
DR MEROPS; C55.001; -.
DR PATRIC; fig|632.152.peg.4449; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR005083; Ser/Thr_AcTrfase.
DR Pfam; PF03421; Acetyltransf_14; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Plasmid; Secreted; Transferase; Virulence.
FT CHAIN 1..288
FT /note="Serine/threonine-protein acetyltransferase YopJ"
FT /id="PRO_0000451623"
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:20430892,
FT ECO:0000305|PubMed:22802624"
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 serine/threonine-protein
FT acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20430892,
FT ECO:0000269|PubMed:22802624"
SQ SEQUENCE 288 AA; 32453 MW; 5A3AFB9F10CA8B78 CRC64;
MIGPISQINI SGGLSEKETS SLISNEELKN IITQLETDIS DGSWFHKNYS RMDVEVMPAL
VIQANNKYPE MNLNLVTSPL DLSIEIKNVI ENGVRSSRFI INMGEGGIHF SVIDYKHING
KTSLILFEPA NFNSMGPAML AIRTKTAIER YQLPDCHFSM VEMDIQRSSS ECGIFSLALA
KKLYIERDSL LKIHEDNIKG ILSDGENPLP HDKLDPYLPV TFYKHTQGKK RLNEYLNTNP
QGVGTVVNKK NETIVNRFDN NKSIVDGKEL SVSVHKKRIA EYKTLLKV
