ID   OSPD3_SHIFL             Reviewed;         565 AA.
AC   Q99Q01; Q7BCM3;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Effector protease OspD3 {ECO:0000305};
DE            EC=3.4.-.- {ECO:0000269|PubMed:32657447};
GN   Name=ospD3 {ECO:0000303|PubMed:32657447};
GN   ORFNames=SF_p0093 {ECO:0000312|EMBL:AAL72316.1};
OS   Shigella flexneri.
OG   Plasmid pCP301.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   CYS-64; HIS-148 AND ASP-171.
RC   STRAIN=YSH6000 / Serotype 2a;
RX   PubMed=32657447; DOI=10.15252/embj.2020104469;
RA   Ashida H., Sasakawa C., Suzuki T.;
RT   "A unique bacterial tactic to circumvent the cell death crosstalk induced
RT   by blockade of caspase-8.";
RL   EMBO J. 39:e104469-e104469(2020).
CC   -!- FUNCTION: Effector protease that disrupts necroptosis in host cells by
CC       mediating proteolytic cleavage of host RIPK1 and RIPK3.
CC       {ECO:0000269|PubMed:32657447}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:32657447}.
CC       Note=Secreted via the type III secretion system (TTSS).
CC       {ECO:0000305|PubMed:32657447}.
CC   -!- DISRUPTION PHENOTYPE: Host cells display necroptosis.
CC       {ECO:0000269|PubMed:32657447}.
CC   -!- SIMILARITY: Belongs to the Toxin_15 family. {ECO:0000305}.
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DR   EMBL; AF386526; AAL72316.1; -; Genomic_DNA.
DR   RefSeq; NP_085251.1; NC_002698.1.
DR   RefSeq; NP_858226.1; NC_004851.1.
DR   RefSeq; WP_010921642.1; NZ_UIPM01000163.1.
DR   RefSeq; YP_009062471.1; NC_024996.1.
DR   SMR; Q99Q01; -.
DR   STRING; 198214.CP0093; -.
DR   EnsemblBacteria; AAL72316; AAL72316; SF_p0093.
DR   GeneID; 1238012; -.
DR   KEGG; sfl:CP0093; -.
DR   PATRIC; fig|198214.7.peg.5346; -.
DR   HOGENOM; CLU_495867_0_0_6; -.
DR   Proteomes; UP000001006; Plasmid pCP301.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR012927; Toxin_15_N.
DR   Pfam; PF07906; Toxin_15; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Plasmid; Protease; Reference proteome; Secreted; Toxin;
KW   Virulence.
FT   CHAIN           1..565
FT                   /note="Effector protease OspD3"
FT                   /id="PRO_0000455088"
FT   MUTAGEN         64
FT                   /note="C->A: Abolished ability to cleave host RIPK1."
FT                   /evidence="ECO:0000269|PubMed:32657447"
FT   MUTAGEN         148
FT                   /note="H->A: Abolished ability to cleave host RIPK1."
FT                   /evidence="ECO:0000269|PubMed:32657447"
FT   MUTAGEN         171
FT                   /note="D->A: Abolished ability to cleave host RIPK1."
FT                   /evidence="ECO:0000269|PubMed:32657447"
SQ   SEQUENCE   565 AA;  63109 MW;  E4F5E1BFDF5D1637 CRC64;
     MPSVNLIPSR KICLQNMINK DNVSVETIQS LLHSKQLPYF SDKRSFLLNL NCQVTDHSGR
     LIVCRHLASY WIAQFNKSSG HVDYHHFAFP DEIKNYVSVS EEEKAINVPA IIYFVENGSW
     GDIIFYIFNE MIFHSEKSRA LEISTSNHNM ALGLKIKETK NGGDFVIQLY DPNHTATHLR
     AEFNKFNLAK IKKLTVDNFL DEKHQKCYGL ISDGMSIFVD RHTPTSMSSI IRWPDNLLHP
     KVIYHAMRMG LTELIQKVTR VVQLSDLSDN TLELLLAAKN DDGLSGLLLA LQNGHSDTIL
     AYGELLETSG LNLDKTVELL TAEGMGGRIS GLSQALQNGH AETIKTYGRL LKKRAINIEY
     NKLKNLLTAY YYDEVHRQIP GLMFALQNGH ADAIRAYGEL ILSPPLLNSE DIVNLLASRR
     YDNVPGLLLA LNNGQADAIL AYGDILNEAK LNLDKKAELL EAKDSNGLSG LFVALHNGCV
     ETIIAYGKIL HTADLTPHQA SKLLAAEGPN GVSGLIIAFQ NRNFEAIKTY MGIIKNENIT
     PEEIAEHLDK KNGSDFLEIM KNIKS