ID   CAP12_NIADE             Reviewed;         312 AA.
AC   A0A1G6LGU2;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=CD-NTase-associated protein 12 {ECO:0000305};
DE            Short=Cap12 {ECO:0000305};
DE   AltName: Full=NAD(+) hydrolase {ECO:0000250|UniProtKB:A0A2T5Y4G4};
DE            EC=3.2.2.5 {ECO:0000250|UniProtKB:A0A2T5Y4G4};
DE   AltName: Full=TIR-STING {ECO:0000303|PubMed:32877915};
DE            Short=NdSTING {ECO:0000303|PubMed:32877915};
GN   Name=cap12 {ECO:0000305}; ORFNames=SAMN04487894_102350;
OS   Niabella drilacis (strain DSM 25811 / CCM 8410 / LMG 26954 / E90).
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niabella.
OX   NCBI_TaxID=1285928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25811 / CCM 8410 / LMG 26954 / E90;
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   C-DI-GMP-BINDING, AND DOMAIN.
RX   PubMed=32877915; DOI=10.1038/s41586-020-2719-5;
RA   Morehouse B.R., Govande A.A., Millman A., Keszei A.F.A., Lowey B., Ofir G.,
RA   Shao S., Sorek R., Kranzusch P.J.;
RT   "STING cyclic dinucleotide sensing originated in bacteria.";
RL   Nature 586:429-433(2020).
RN   [3]
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 I-D CBASS(GG) system (PubMed:32839535).
CC       {ECO:0000303|PubMed:32839535, ECO:0000305|PubMed:32877915}.
CC   -!- FUNCTION: The effector protein for this CBASS system. Binds c-di-GMP,
CC       does not bind cUMP-AMP (PubMed:32877915). Upon activation by c-di-GMP
CC       forms filaments which hydrolyze NAD(+); filament formation is required
CC       for enzyme activation (By similarity).
CC       {ECO:0000250|UniProtKB:A0A2T5Y4G4, ECO:0000269|PubMed:32877915}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC         Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.5;
CC         Evidence={ECO:0000250|UniProtKB:A0A2T5Y4G4};
CC   -!- ACTIVITY REGULATION: NAD(+) hydrolase activity is strongly stimulated
CC       by c-di-GMP, weakly by 3'3'-cGAMP, very weakly by c-di-AMP but not at
CC       all by 2'3'-cGAMP (Probable). Self-association of TIR domains is
CC       required for NADase activity (By similarity).
CC       {ECO:0000250|UniProtKB:A0A2T5Y4G4, ECO:0000305|PubMed:32877915}.
CC   -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity. The
CC       cyclic nucleotide binds in the C-terminal bacterial STING region.
CC       {ECO:0000305|PubMed:32877915}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the bacterial STING
CC       family. {ECO:0000305}.
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DR   EMBL; FMZO01000002; SDC42652.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6LGU2; -.
DR   SMR; A0A1G6LGU2; -.
DR   STRING; 1285928.SAMN04487894_102350; -.
DR   EnsemblBacteria; SDC42652; SDC42652; SAMN04487894_102350.
DR   OMA; FEVTIWN; -.
DR   Proteomes; UP000198757; Unassembled WGS sequence.
DR   GO; GO:0061810; F:NAD glycohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR019302; TIR-like_dom.
DR   Pfam; PF10137; TIR-like; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..312
FT                   /note="CD-NTase-associated protein 12"
FT                   /id="PRO_0000451880"
FT   DOMAIN          5..127
FT                   /note="TIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204,
FT                   ECO:0000305|PubMed:32877915"
SQ   SEQUENCE   312 AA;  35580 MW;  9BFACDC215ABB8B4 CRC64;
     MIKKRLFIGS SSEELKTAEI VKEVLLKDFE VTIWNDNVWD TAVFKINQNF LADLLKASLQ
     FDFGILIGTK DDKVMFREVE MIQPRDNVLF ELGLFTGRLG TSKCAFLIDK EIKLPSDFNG
     LTLARFDSTN EATVIAGANS IKDLFLASAD DEINFFPSAT LASVYYENLI VPICRFIIDN
     NGFTKGDTHY QKCKLNIIVP ERINQDVNLQ FEKLKGLFTT ENVSFKYSGR PRQISVDTQI
     KNDTLEFIDF PTIITGINHA ISNLLPNDFN KQSPDYSSIL DRELRRFITT LKKLLIRGGF
     DEMVNVKRDS EL