OSPC1_SHIFL
ID OSPC1_SHIFL Reviewed; 470 AA.
AC Q8VSJ7; A0A2S4MRB8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Arginine ADP-riboxanase OspC1 {ECO:0000305};
DE EC=4.3.99.- {ECO:0000269|PubMed:34671164};
GN Name=ospC1 {ECO:0000303|PubMed:23684308};
GN ORFNames=SF_p0094 {ECO:0000312|EMBL:AAL72322.1};
OS Shigella flexneri.
OG Plasmid pCP301, Plasmid pMYSH6000, and Plasmid pWR100.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=YSH6000 / Serotype 2a; PLASMID=pMYSH6000;
RX PubMed=23684308; DOI=10.1016/j.chom.2013.04.012;
RA Kobayashi T., Ogawa M., Sanada T., Mimuro H., Kim M., Ashida H.,
RA Akakura R., Yoshida M., Kawalec M., Reichhart J.M., Mizushima T.,
RA Sasakawa C.;
RT "The Shigella OspC3 effector inhibits caspase-4, antagonizes inflammatory
RT cell death, and promotes epithelial infection.";
RL Cell Host Microbe 13:570-583(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
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 [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; PLASMID=pWR100;
RX PubMed=16988276; DOI=10.1128/iai.00594-06;
RA Zurawski D.V., Mitsuhata C., Mumy K.L., McCormick B.A., Maurelli A.T.;
RT "OspF and OspC1 are Shigella flexneri type III secretion system effectors
RT that are required for postinvasion aspects of virulence.";
RL Infect. Immun. 74:5964-5976(2006).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=34671164; DOI=10.1038/s41586-021-04020-1;
RA Li Z., Liu W., Fu J., Cheng S., Xu Y., Wang Z., Liu X., Shi X., Liu Y.,
RA Qi X., Liu X., Ding J., Shao F.;
RT "Shigella evades pyroptosis by arginine ADP-riboxanation of caspase-11.";
RL Nature 599:290-295(2021).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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: ADP-riboxanase effector that mediates arginine ADP-
CC riboxanation of host target protein(s) (PubMed:34671164). Inhibits host
CC CASP8 and apoptotic host cell death, possibly by catalyzing its ADP-
CC riboxanation (PubMed:32657447). Does not catalyze ADP-riboxanation of
CC host CASP4/CASP11 (PubMed:34671164). {ECO:0000269|PubMed:32657447,
CC ECO:0000269|PubMed:34671164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + NAD(+) = ADP-riboxanated L-argininyl-
CC [protein] + H(+) + NH4(+) + nicotinamide; Xref=Rhea:RHEA:69500,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17719, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:28938, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:184300;
CC Evidence={ECO:0000269|PubMed:34671164};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69501;
CC Evidence={ECO:0000269|PubMed:34671164};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16988276,
CC ECO:0000269|PubMed:23684308}. Host nucleus
CC {ECO:0000269|PubMed:16988276}. Note=Secreted via the type III secretion
CC system (TTSS). {ECO:0000269|PubMed:16988276,
CC ECO:0000269|PubMed:23684308}.
CC -!- DISRUPTION PHENOTYPE: Host cells display apoptosis caused by strongly
CC increased CASP8 activation. {ECO:0000269|PubMed:32657447}.
CC -!- SIMILARITY: Belongs to the OspC family. {ECO:0000305}.
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DR EMBL; AB819725; BAN28453.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72322.1; -; Genomic_DNA.
DR RefSeq; NP_858227.1; NC_004851.1.
DR RefSeq; WP_001026857.1; NZ_WPGS01000178.1.
DR SMR; Q8VSJ7; -.
DR STRING; 198214.CP0094; -.
DR EnsemblBacteria; AAL72322; AAL72322; SF_p0094.
DR GeneID; 1238025; -.
DR KEGG; sfl:CP0094; -.
DR PATRIC; fig|198214.7.peg.5347; -.
DR HOGENOM; CLU_053336_0_0_6; -.
DR OMA; SIANQKE; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140740; F:ADP-riboxanase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0052041; P:negative regulation by symbiont of host programmed cell death; IDA:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR010366; OspC1-3.
DR Pfam; PF06128; Shigella_OspC; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Host nucleus; Lyase; Plasmid; Reference proteome; Repeat;
KW Secreted; Toxin; Virulence.
FT CHAIN 1..470
FT /note="Arginine ADP-riboxanase OspC1"
FT /id="PRO_0000455082"
FT REPEAT 363..392
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 399..431
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 438..467
FT /note="ANK 3"
FT /evidence="ECO:0000255"
SQ SEQUENCE 470 AA; 53946 MW; 8A8F522DAA13F219 CRC64;
MNISETLNSA NTQCNIDSMD NRLHTLFPKV TSVRNAAQQT MPDEKNLKDS ANIIKSFFRK
TIAAQSYSRM FSQGSNFKSL NIAIDAPSDA KASFKAIEHL DRLSKHYISE IREKLHPLSA
EELNLLSLII NSDLIFRHQS NSDLSDKILN IKSFNKIQSE GICTKRNTYA DDIKKIANHD
FVFFGVEISN HQKKHPLNTK HHTVDFGANA YIIDHDSPYG YMTLTDHFDN AIPPVFYHEH
QSFLDKFSEV NKEVSRYVHG SKGIIDVPIF NTKDMKLGLG LYLIDFIRKS EDQSFKEFCY
GKNLAPVDLD RIINFVFQPE YHIPRMVSTE NFKKVKIREI SLEEAVTASN YEEINKQVTN
KKIALQALFL SITNQKEDVA LYILSNFEIT RQDVISIKHE LYDIEYLLSA HNSSCKVLEY
FINKGLVDVN TKFKKTNSGD CMLDNAIKYE NAEMIKLLLK YGATSDNKYI
