ID   CDNG_ROSEK              Reviewed;         376 AA.
AC   A0A150XSC5;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   08-JUN-2016, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=c-di-GMP synthase {ECO:0000303|PubMed:32877915};
DE            EC=2.7.7.65 {ECO:0000269|PubMed:32877915};
DE   AltName: Full=ReCdnE {ECO:0000303|PubMed:32877915};
DE   AltName: Full=ReCdnG {ECO:0000305};
DE   AltName: Full=cGAS/DncV-like nucleotidyltransferase;
DE            Short=CD-NTase;
GN   Name=cdnG {ECO:0000303|PubMed:32877915}; ORFNames=MB14_13780;
OS   Roseivirga ehrenbergii (strain DSM 102268 / JCM 13514 / KCTC 12282 / NCIMB
OS   14502 / KMM 6017).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Roseivirgaceae;
OC   Roseivirga.
OX   NCBI_TaxID=279360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 102268 / JCM 13514 / KCTC 12282 / NCIMB 14502 / KMM 6017;
RA   Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G., Chong C.S.;
RT   "Genome sequencing of Roseivirga ehrenbergii KMM 6017.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
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: Cyclic dinucleotide synthase that catalyzes the synthesis of
CC       c-di-GMP, has no activity with other NTP substrates.
CC       {ECO:0000269|PubMed:32877915}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 GTP = cyclic di-3',5'-guanylate + 2 diphosphate;
CC         Xref=Rhea:RHEA:24898, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:58805; EC=2.7.7.65;
CC         Evidence={ECO:0000269|PubMed:32877915};
CC   -!- MISCELLANEOUS: Bacteria with this enzyme do not have other c-di-GMP
CC       synthase enzymes (no GGDEF or EAL-domain containing proteins),
CC       suggesting this second messenger has been co-opted for CBASS signaling
CC       via STING activation. {ECO:0000305|PubMed:32877915}.
CC   -!- SIMILARITY: Belongs to the CD-NTase family. G05 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; LQZQ01000002; KYG81647.1; -; Genomic_DNA.
DR   RefSeq; WP_062588800.1; NZ_SMGS01000002.1.
DR   AlphaFoldDB; A0A150XSC5; -.
DR   SMR; A0A150XSC5; -.
DR   EnsemblBacteria; KYG81647; KYG81647; MB14_13780.
DR   OMA; FYPQGSM; -.
DR   Proteomes; UP000075583; Unassembled WGS sequence.
DR   GO; GO:0052621; F:diguanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR   InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
PE   1: Evidence at protein level;
KW   Antiviral defense; GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..376
FT                   /note="c-di-GMP synthase"
FT                   /id="PRO_0000451885"
SQ   SEQUENCE   376 AA;  43174 MW;  73090D073B6AEB65 CRC64;
     MLITSNAKTQ LEDTLAKMAE AAELDKTRWS RLNTAYEAIS KWLSDDPEFF GGVEIEIYPQ
     GSVSIGTTTK PYGKTEFDLD VVIHIKLLSS NYDPKTIFNE VVRRLNENET YRKICEPKSR
     CVRLNYQGDF HLDVVPGCMV IIYNHELIDI TDQKNEIWLR SSPKGYQKWF LDIANRVELT
     LLEMTFSAHK VEIEEYAKKK PLQRAVQLIK MRRNIYFDQN PENAPTSIIL TTLAAQFYEG
     QSSISETFEG IISKLKNHIE TLFPNRPFEL PNPVNPSENL ADIWVDKPEL YKHFISFINN
     LHNEWQDLKK AHGIEEEAIL MKGMFGNDPY IKAMEARAET VNQKRGNGLG ILATGVMVDR
     AVEKSLPVMP NTFYGD