OSPC2_SHIFL
ID OSPC2_SHIFL Reviewed; 484 AA.
AC Q8VSL8; A0A2G3EFG7; A0A2S4MRJ2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Arginine ADP-riboxanase OspC2 {ECO:0000305};
DE EC=4.3.99.- {ECO:0000269|PubMed:34671164};
GN Name=ospC2 {ECO:0000303|PubMed:23684308};
GN ORFNames=SF_p0063 {ECO:0000312|EMBL:AAL72320.1};
OS Shigella flexneri.
OG Plasmid pCP301, and Plasmid pMYSH6000.
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 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).
CC -!- FUNCTION: ADP-riboxanase effector that mediates arginine ADP-
CC riboxanation of host target protein(s) (PubMed:34671164). Does not
CC catalyze ADP-riboxanation of host CASP4/CASP11 (PubMed:34671164).
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:23684308}.
CC Note=Secreted via the type III secretion system (TTSS).
CC {ECO:0000269|PubMed:23684308}.
CC -!- SIMILARITY: Belongs to the OspC family. {ECO:0000305}.
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DR EMBL; AF386526; AAL72320.1; -; Genomic_DNA.
DR EMBL; AB819726; BAN28454.1; -; Genomic_DNA.
DR RefSeq; NP_858196.1; NC_004851.1.
DR RefSeq; WP_000701108.1; NZ_WPGT01000228.1.
DR SMR; Q8VSL8; -.
DR STRING; 198214.CP0063; -.
DR EnsemblBacteria; AAL72320; AAL72320; SF_p0063.
DR GeneID; 1238023; -.
DR KEGG; sfl:CP0063; -.
DR PATRIC; fig|198214.7.peg.5305; -.
DR HOGENOM; CLU_053336_0_0_6; -.
DR OMA; TAMWHAI; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0140740; F:ADP-riboxanase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR010366; OspC1-3.
DR Pfam; PF06128; Shigella_OspC; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Lyase; Plasmid; Reference proteome; Repeat; Secreted; Toxin;
KW Virulence.
FT CHAIN 1..484
FT /note="Arginine ADP-riboxanase OspC2"
FT /id="PRO_0000455083"
FT REPEAT 414..444
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 451..480
FT /note="ANK 2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 484 AA; 55551 MW; DE166153D46E66AE CRC64;
MKIPEAVNHI NVQNNIDLVD GKINPNKDTK ALQKNISCVT NSSSSGISEK HLDHCADTVK
SFLRKSIAAQ SYSKMFSQGT SFKSLNLSIE APSGARSSFR SLEHLDKVSR HYLSEIIQKT
HPLSSDERHL LSIIINSDFN FRHQSNANLS NNTLNIKSFD KIKSENIQTY KNTFSEDIEE
IANHDFVFFG VEISNHQETL PLNKTHHTVD FGANAYIIDH DSPYGYMTLT DHFDNAIPPV
FYHEHQSFFL DNFKEVVDEV SRYVHGNQGK TDVPIFNTKD MRLGIGLHLI DFIRKSKDQR
FREFCYNKNI DPVSLDRIIN FVFQLEYHIP RMLSTDNFKK IRLRDISLED AIKASNYEEI
NNKVTDKKMA HQALAYSLGN AKSDMALYLL SKFNFTKQDI AEMEKMNNNM YCELYDVEYL
LSEDSANYKV LEYFISNGLV DVNKRFQKAN SGDTMLDNAM KSKDSKTIDF LLKNGAVSGK
RFGR