ID   CAP3_ECOLX              Reviewed;         156 AA.
AC   P0DTF3;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 1.
DT   03-AUG-2022, entry version 7.
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   ORFNames=ESG_RS0100125, geneD {ECO:0000303|PubMed:31533127};
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=TW11681;
RX   PubMed=21078854; DOI=10.1128/iai.00932-10;
RA   Sahl J.W., Steinsland H., Redman J.C., Angiuoli S.V., Nataro J.P.,
RA   Sommerfelt H., Rasko D.A.;
RT   "A comparative genomic analysis of diverse clonal types of enterotoxigenic
RT   Escherichia coli reveals pathovar-specific conservation.";
RL   Infect. Immun. 79:950-960(2011).
RN   [2]
RP   ANTIVIRAL DEFENSE, NOMENCLATURE, OPERON STRUCTURE, AND MUTAGENESIS OF
RP   GLU-38.
RC   STRAIN=TW11681;
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   NOMENCLATURE.
RC   STRAIN=TW11681;
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 infection. When capV and dncV
CC       are introduced in E.coli MG1655 there is 1000-fold protection against
CC       phage P1; protection against other phage (T4, T5 and T6) requires the 2
CC       subsequent genes. {ECO:0000269|PubMed:31533127}.
CC   -!- INDUCTION: Part of the CBASS operon consisting of capV-dncV-cap2-cap3.
CC       {ECO:0000305|PubMed:31533127}.
CC   -!- MISCELLANEOUS: The sequence of this protein is available under the NCBI
CC       RefSeq accession WP_024167427.1. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M67B family. {ECO:0000305}.
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DR   EMBL; AELD01000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_024167427.1; NZ_VTME01000123.1.
DR   AlphaFoldDB; P0DTF3; -.
DR   SMR; P0DTF3; -.
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   1: Evidence at protein level;
KW   Antiviral defense; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Zinc.
FT   CHAIN           1..156
FT                   /note="CD-NTase-associated protein 3"
FT                   /id="PRO_0000451858"
FT   DOMAIN          9..147
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   ACT_SITE        38
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:D4GTS4"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1Y4"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1Y4"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1Y4"
FT   MUTAGEN         38
FT                   /note="E->A: Loss of defense against phage T4, T5 and T6."
FT                   /evidence="ECO:0000269|PubMed:31533127"
SQ   SEQUENCE   156 AA;  18095 MW;  5CEE31FC7BE55D2C CRC64;
     MNMNELVFID DFDNHVVIMS EVVMRLNSYR QTHYTSTESG GTLIGERRGQ HLVITHISEP
     GQDDVRNRTG LERKGIHHQQ KVNDLFQQSN GFIVYLGEWH THPEDFPHPS FIDIKSWVMG
     IVATEPMIML IVGRKDIWIG KKIKNDIKKL KKKMVS