CAP3_VIBCH
ID CAP3_VIBCH Reviewed; 156 AA.
AC Q9KVG5;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=CD-NTase-associated protein 3 {ECO:0000303|PubMed:32544385};
DE AltName: Full=Probable metalloprotease Cap3 {ECO:0000305};
GN Name=cap3 {ECO:0000303|PubMed:32544385};
GN OrderedLocusNames=VC_0181 {ECO:0000312|EMBL:AAF93357.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP ANTIVIRAL DEFENSE, AND OPERON STRUCTURE.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=31533127; DOI=10.1038/s41586-019-1605-5;
RA Cohen D., Melamed S., Millman A., Shulman G., Oppenheimer-Shaanan Y.,
RA Kacen A., Doron S., Amitai G., Sorek R.;
RT "Cyclic GMP-AMP signalling protects bacteria against viral infection.";
RL Nature 574:691-695(2019).
RN [3]
RP ANTIVIRAL DEFENSE, NOMENCLATURE, AND OPERON STRUCTURE.
RC STRAIN=El Tor C6706;
RX PubMed=32544385; DOI=10.1016/j.cell.2020.05.019;
RA Lowey B., Whiteley A.T., Keszei A.F.A., Morehouse B.R., Antine S.P.,
RA Cabrera V.J., Kashin D., Schwede F., Mekalanos J.J., Shao S., Lee A.S.Y.,
RA Kranzusch P.J.;
RT "CBASS immunity uses CARF-related effectors to sense 3'-5' and 2'-5'-linked
RT cyclic oligonucleotide signals and protect bacteria from phage infection.";
RL Cell 182:38-49(2020).
RN [4]
RP CLASSIFICATION AND NOMENCLATURE.
RX PubMed=32839535; DOI=10.1038/s41564-020-0777-y;
RA Millman A., Melamed S., Amitai G., Sorek R.;
RT "Diversity and classification of cyclic-oligonucleotide-based anti-phage
RT signalling systems.";
RL Nat. Microbiol. 5:1608-1615(2020).
CC -!- FUNCTION: CBASS (cyclic oligonucleotide-based antiphage signaling
CC system) provides immunity against bacteriophage. The CD-NTase protein
CC synthesizes cyclic nucleotides in response to infection; these serve as
CC specific second messenger signals. The signals activate a diverse range
CC of effectors, leading to bacterial cell death and thus abortive phage
CC infection. A type II-A(GA) CBASS system (PubMed:32839535).
CC {ECO:0000269|PubMed:31533127, ECO:0000303|PubMed:32839535}.
CC -!- FUNCTION: Protects E.coli against phage P1 and T2 infection. When the 4
CC gene operon capV-dncV-cap2-cap3 is introduced in E.coli MG1655 there is
CC about 100-fold protection against phages P1 and T2 (PubMed:31533127).
CC Protects E.coli against phage T2 infection. When the CBASS operon
CC (capV-dcnV-cap2-cap3) is introduced in E.coli MG1655 there is a more
CC than 10(3) decrease in the efficiency of T2 plaque formation. Protects
CC 100-fold against phage T5, offers no protection against T7
CC (PubMed:32544385). {ECO:0000269|PubMed:31533127,
CC ECO:0000269|PubMed:32544385}.
CC -!- INDUCTION: Part of the CBASS operon consisting of capV-dncV-cap2-cap3.
CC {ECO:0000305|PubMed:31533127, ECO:0000305|PubMed:32544385}.
CC -!- SIMILARITY: Belongs to the peptidase M67B family. {ECO:0000305}.
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DR EMBL; AE003852; AAF93357.1; -; Genomic_DNA.
DR PIR; H82354; H82354.
DR RefSeq; NP_229838.1; NC_002505.1.
DR AlphaFoldDB; Q9KVG5; -.
DR SMR; Q9KVG5; -.
DR STRING; 243277.VC_0181; -.
DR PRIDE; Q9KVG5; -.
DR DNASU; 2614172; -.
DR EnsemblBacteria; AAF93357; AAF93357; VC_0181.
DR KEGG; vch:VC_0181; -.
DR eggNOG; COG1310; Bacteria.
DR HOGENOM; CLU_123228_1_0_6; -.
DR OMA; HTHPEPH; -.
DR BioCyc; VCHO:VC0181-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR011952; CAP3.
DR InterPro; IPR028090; JAB_dom_prok.
DR Pfam; PF14464; Prok-JAB; 1.
DR PIRSF; PIRSF028170; CHP02256; 1.
DR TIGRFAMs; TIGR02256; ICE_VC0181; 1.
PE 3: Inferred from homology;
KW Antiviral defense; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..156
FT /note="CD-NTase-associated protein 3"
FT /id="PRO_0000451859"
FT DOMAIN 9..147
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT ACT_SITE 39
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:D4GTS4"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8U1Y4"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8U1Y4"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8U1Y4"
SQ SEQUENCE 156 AA; 18065 MW; 8D437D0BBD0A2DC3 CRC64;
MMSDVELVFK DESDCLVVIM GHVVTRLLSY RQLHHLTPES AGVLIGERRG QHLVVCDISE
PGSGDIRQRC RVDRRGVHHQ SRVNEAFERS AGTHLYLGEW HTHPEDRPFP SATDRHSWRR
NIVSDESMLL LIVGRKDFWL GKKERELITV FKKIES
