ID   OSPC3_ECOLX             Reviewed;         484 AA.
AC   P0DV36;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 1.
DT   03-AUG-2022, entry version 3.
DE   RecName: Full=Arginine ADP-riboxanase OspC3 {ECO:0000305};
DE            EC=4.3.99.- {ECO:0000269|PubMed:34671164};
GN   Name=ospC3 {ECO:0000303|PubMed:34671164};
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFSAN029787;
RA   Timme R., Allard M.W., Strain E., Evans P.S., Brown E.;
RT   "Whole genome shotgun sequencing of cultured foodborne pathogen.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-192 AND HIS-328.
RC   STRAIN=CFSAN029787;
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 inhibits host cell pyroptosis
CC       (PubMed:34671164). Acts by mediating arginine ADP-riboxanation of host
CC       CASP4/CASP11, blocking CASP4/CASP11 autoprocessing (PubMed:34671164).
CC       This prevents CASP4 activation and ability to recognize and cleave
CC       GSDMD, thereby inhibiting LPS-induced pyroptosis (By similarity). ADP-
CC       riboxanation takes place in two steps: OspC3 first catalyzes ADP-
CC       ribosylation of target Arg, and then initiates a deamination to remove
CC       one N-omega group (By similarity). {ECO:0000250|UniProtKB:A0A0H2US87,
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:0000250|UniProtKB:A0A0H2US87}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:A0A0H2US87}. Note=Secreted via the
CC       type III secretion system (TTSS). {ECO:0000250|UniProtKB:A0A0H2US87}.
CC   -!- SIMILARITY: Belongs to the OspC family. {ECO:0000305}.
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DR   EMBL; CP011417; AKH27395.1; -; Genomic_DNA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0140740; F:ADP-riboxanase activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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.
PE   1: Evidence at protein level;
KW   ANK repeat; Host cytoplasm; Lyase; Repeat; Secreted; Toxin; Virulence.
FT   CHAIN           1..484
FT                   /note="Arginine ADP-riboxanase OspC3"
FT                   /id="PRO_0000455085"
FT   REPEAT          369..398
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          413..444
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          451..480
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         192
FT                   /note="E->A: In EH/AA mutant; abolished arginine ADP-
FT                   riboxanation of host CASP4/CASP11; when associated with A-
FT                   328."
FT                   /evidence="ECO:0000269|PubMed:34671164"
FT   MUTAGEN         328
FT                   /note="H->A: In EH/AA mutant; abolished arginine ADP-
FT                   riboxanation of host CASP4/CASP11; when associated with A-
FT                   192."
FT                   /evidence="ECO:0000269|PubMed:34671164"
SQ   SEQUENCE   484 AA;  55610 MW;  063E45915DDCA852 CRC64;
     MKIPEAVNHI NVQNNIDLVD GKTNPNKATK ALQKNILRVT NSSSSGISEK HLDHCANTVK
     NFLRKSIAAQ SYSKMFSQGT SFKSLNLSIE APSGARSSFR SLEHLDKVSR HYISEIIQKV
     HPLSSDERLL LSIIINSNFN FRHQSNSNLS NNILNIKSFD KMQSENIQTH KNTYSEDIKE
     ISNHDFVFFG VEISNHQEKL PLNKTHHTVD FGANAYIIDH DSPYGYMTLT DHFDNAIPPV
     FYHEHQSFFL DNFKEVVDEV SRYVHGNQGK TDVPIFNTKD MRLGIGLHLI DFIRKSKDQG
     FREFCYNKNI DPVSLDRIIN FVFQLEYHIP RMLSTDNFKK IKLRDISLED AIKASNYEEI
     NNKVTDKKMA HQALAYSLGN KKADIALYLL SKFNFTKQDV AEMEKMNNNR YCNLYDVEYL
     LSKDGANYKV LEYFINNGLV DVNKKFQKAN SGDTMLDNAM KSKDSKMIDF LLKNGAILGK
     RFEI