(data stored in ACNUC9435 zone)

SWISSPROT: YOPJ_YERPS

ID   YOPJ_YERPS              Reviewed;         288 AA.
AC   P31498; Q663G8; Q6J1F6;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 3.
DT   11-DEC-2019, entry version 99.
DE   RecName: Full=Effector protein YopJ;
DE   AltName: Full=Virulence factor YopJ;
GN   Name=yopJ; OrderedLocusNames=pYV0098;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OG   Plasmid pIB1, and Plasmid pYV.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-11.
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 [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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-264.
RC   PLASMID=pIB1;
RX   PubMed=1840573;
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   [5]
RP   FUNCTION.
RX   PubMed=11834367; DOI=10.1016/s1369-5274(02)00283-7;
RA   Orth K.;
RT   "Function of the Yersinia effector YopJ.";
RL   Curr. Opin. Microbiol. 5:38-43(2002).
RN   [6]
RP   FUNCTION.
RX   PubMed=12433923; DOI=10.1074/jbc.m209905200;
RA   Yoon S., Liu Z., Eyobo Y., Orth K.;
RT   "Yersinia effector YopJ inhibits yeast MAPK signaling pathways by an
RT   evolutionarily conserved mechanism.";
RL   J. Biol. Chem. 278:2131-2135(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=16301742; DOI=10.1084/jem.20051194;
RA   Zhou H., Monack D.M., Kayagaki N., Wertz I., Yin J., Wolf B., Dixit V.M.;
RT   "Yersinia virulence factor YopJ acts as a deubiquitinase to inhibit NF-
RT   kappa B activation.";
RL   J. Exp. Med. 202:1327-1332(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=16728640; DOI=10.1126/science.1126867;
RA   Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J.,
RA   Orth K.;
RT   "Yersinia YopJ acetylates and inhibits kinase activation by blocking
RT   phosphorylation.";
RL   Science 312:1211-1214(2006).
RN   [9]
RP   FUNCTION.
RA   Orth K.;
RL   Unpublished observations (JUL-2006).
CC   -!- FUNCTION: Blocks the innate immune response by blocking cytokine
CC       production and inducing apoptosis in the infected cells. Inhibits the
CC       MAPK and NF-kappa-B signaling pathways by acetylating MAP2K1, MAP2K6
CC       and probably also MAP2K3, MAP2K4 and I-kappa-B kinase on residues
CC       critical for their activation by phosphorylation, thus preventing it.
CC       {ECO:0000269|PubMed:11834367, ECO:0000269|PubMed:12433923,
CC       ECO:0000269|PubMed:16301742, ECO:0000269|PubMed:16728640,
CC       ECO:0000269|Ref.9}.
CC   -!- SUBUNIT: Interacts with human MAP2K1, MAP2K3, MAP2K4, MAP2K6 and IKBKB.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III secretion
CC       system (TTSS).
CC   -!- INDUCTION: At 37 degrees Celsius in the absence of calcium.
CC   -!- SIMILARITY: Belongs to the peptidase C55 family. {ECO:0000305}.
CC   -!- CAUTION: Thought first to be a protease involved in de-ubiquitination,
CC       latest evidence shows that YopJ is an acetyltransferase that uses a
CC       dual substrate mechanism similar to the one used by papain-like
CC       proteases. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA27659.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA68488.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; L33833; AAA68488.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AY606230; AAT28340.1; -; Genomic_DNA.
DR   EMBL; BX936399; CAF25441.1; -; Genomic_DNA.
DR   EMBL; M58506; AAA27659.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; WP_002225474.1; NZ_CP009711.1.
DR   SMR; P31498; -.
DR   DIP; DIP-61317N; -.
DR   IntAct; P31498; 1.
DR   MEROPS; C55.001; -.
DR   EnsemblBacteria; CAF25441; CAF25441; pYV0098.
DR   GeneID; 39573280; -.
DR   KEGG; ypo:BZ17_4238; -.
DR   KEGG; yps:pYV0098; -.
DR   PATRIC; fig|273123.14.peg.4473; -.
DR   HOGENOM; HOG000219637; -.
DR   KO; K08598; -.
DR   OMA; HRKRATE; -.
DR   BRENDA; 3.4.22.B19; 4560.
DR   Proteomes; UP000001011; Plasmid pYV.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR005083; Ser/Thr_AcTrfase.
DR   Pfam; PF03421; Acetyltransf_14; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P31498.
DR   SWISS-2DPAGE; P31498.
KW   Acyltransferase; Direct protein sequencing; Plasmid; Secreted; Transferase;
KW   Virulence.
FT   CHAIN           1..288
FT                   /note="Effector protein YopJ"
FT                   /id="PRO_0000066368"
FT   ACT_SITE        172
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
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
//

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