ID   OSPC3_CHRS5             Reviewed;         487 AA.
AC   A0A2H5DV25;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   03-AUG-2022, entry version 13.
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}; ORFNames=CXB49_08835;
OS   Chromobacterium sp. (strain ATCC 53434 / SC 14030).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium; unclassified Chromobacterium.
OX   NCBI_TaxID=2059672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53434 / SC 14030;
RA   Pishchany G., Koren S., Kolter R.;
RT   "Whole genome sequence of Chromobacterium ATCC 53434.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-187 AND HIS-327.
RC   STRAIN=ATCC 53434 / SC 14030;
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; CP025429; AUH50908.1; -; Genomic_DNA.
DR   EnsemblBacteria; AUH50908; AUH50908; CXB49_08835.
DR   KEGG; chro:CXB49_08835; -.
DR   Proteomes; UP000234260; Chromosome.
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; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR010366; OspC1-3.
DR   Pfam; PF13606; Ank_3; 1.
DR   Pfam; PF06128; Shigella_OspC; 1.
DR   SMART; SM00248; ANK; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Host cytoplasm; Lyase; Repeat; Secreted; Toxin; Virulence.
FT   CHAIN           1..487
FT                   /note="Arginine ADP-riboxanase OspC3"
FT                   /id="PRO_0000455084"
FT   REPEAT          368..398
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          444..473
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         187
FT                   /note="E->A: In EH/AA mutant; abolished arginine ADP-
FT                   riboxanation of host CASP4/CASP11; when associated with A-
FT                   327."
FT                   /evidence="ECO:0000269|PubMed:34671164"
FT   MUTAGEN         327
FT                   /note="H->A: In EH/AA mutant; abolished arginine ADP-
FT                   riboxanation of host CASP4/CASP11; when associated with A-
FT                   187."
FT                   /evidence="ECO:0000269|PubMed:34671164"
SQ   SEQUENCE   487 AA;  53542 MW;  E163B5290BEAF3A2 CRC64;
     MRVETHSPSF TNPNPAEACS GDPTEMGSRL SGVSRAPLPH AAAGRDGEAA AAGKIGAFLR
     KAVAAQSYGL MFANGKLFEA TGDALEKREQ YGFSALKRLD GLSRRNLDAV AARLGALDSA
     EQALKQHIMA GAWHFRHQSN AALDDGEKAT IASNHLLSRQ ARSSGGNTFA DDKALLSNHD
     FVFFGVEFSG RDKNDKPLNH KHSTMDFGAN AYVVSDALPA CRNGYLTLTD HFFNRVPGGR
     EAEHQDFVGR FAQMGRESGR WIHEGKYRQN APLFCYRDMK AAVALHLIEF MRNSQDEAFK
     AYVFDQATQS GPALDRVLNS VFQAEFHIPR LMATTDYAKH PLRPMLLKEA VDSVNLPALS
     DLVSNRGDAV TAMWHAINKG KDEVVAYLLG NWQFEAKDFS HAPAGFYHEL NYALSESGAS
     VYILDQFLSR GWAAVNAPFE HVNRGDTMLD NAVKYGNREM VAALIKHGAD RNLLSKWHKS
     DLDALLA