COPC_CHRVO
ID COPC_CHRVO Reviewed; 487 AA.
AC Q7NWF2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Arginine ADP-riboxanase CopC {ECO:0000305};
DE EC=4.3.99.- {ECO:0000269|PubMed:34671164};
GN Name=copC {ECO:0000303|PubMed:34671164}; OrderedLocusNames=CV_2038;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-187 AND HIS-327.
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
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 (PubMed:34671164).
CC ADP-riboxanation takes place in two steps: CopC 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; AE016825; AAQ59710.1; -; Genomic_DNA.
DR SMR; Q7NWF2; -.
DR EnsemblBacteria; AAQ59710; AAQ59710; CV_2038.
DR KEGG; cvi:CV_2038; -.
DR eggNOG; ENOG502ZC73; Bacteria.
DR HOGENOM; CLU_053336_0_0_4; -.
DR OMA; TAMWHAI; -.
DR Proteomes; UP000001424; 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; PF06128; Shigella_OspC; 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; Reference proteome; Repeat; Secreted;
KW Toxin; Virulence.
FT CHAIN 1..487
FT /note="Arginine ADP-riboxanase CopC"
FT /id="PRO_0000455087"
FT REPEAT 368..398
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 444..476
FT /note="ANK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023"
FT REGION 1..27
FT /note="Disordered"
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; 52911 MW; 0A803B4139D64819 CRC64;
MRVENHSPSL SKLNPPEAGS GDPTAIGRRL SGIRRAPLPH VSAGSDGEAA AAGKIGAFLR
KAVAAQSYGL MFANGKLFEA TGDALEKRGQ YGFSALQRLD GLSRRNLAAV EARLGALDSA
ERGLKERIMT GAWHFRHQSN AALDDGKTAA IASNHLLARE SRSSGGNTFA GDKALLSNHD
FVFFGVEFSG RGKQDKPLNH KHSTMDFGAN AYVVPDTLPA CRHGYLTLTD HFFNRVPGGR
EAEHQDFVGS FPQMGAETGR WIHEGKYRQN APIFNYRDMK AAVALHLIEF LRDSKDAAFK
AYVFDQAMQS GQALDRVLNS VFQAEFHIPR LMATTDYAKH PLRPMLLKEA VDSVNLPALS
GLVSSKGDAV TAMWHAIDKG KDAVAAHLLG NWRFEAGDFA SAPPGFYHEL NYALSEHGAS
VYILDQFLSR GWAAVNAPFE HVNSGETMLD NAVKYGNREM AAALIKHGAD RNLLSEWNGG
KLDALLA
