ID   CDNE_LACSX              Reviewed;         346 AA.
AC   P0DUE3;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=c-di-GMP synthase {ECO:0000303|PubMed:32877915};
DE            EC=2.7.7.65 {ECO:0000269|PubMed:32877915};
DE   AltName: Full=LbCdnE {ECO:0000303|PubMed:32877915};
DE   AltName: Full=cGAS/DncV-like nucleotidyltransferase;
DE            Short=CD-NTase;
GN   Name=cdnE {ECO:0000303|PubMed:32877915};
GN   ORFNames=Ga0313508_15008, IMG 2800731184;
OS   Lachnospiraceae bacterium (strain RUG226).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=2778090;
RN   [1]
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   [2]
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(GG) CBASS 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. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=IMG gene page for 2800731184;
CC       URL="https://img.jgi.doe.gov/cgi-bin/m/main.cgi?section=GeneDetail&page=genePageMainFaa&gene_oid=2800731184";
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DR   AlphaFoldDB; P0DUE3; -.
DR   SMR; P0DUE3; -.
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   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR043519; NT_sf.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN           1..346
FT                   /note="c-di-GMP synthase"
FT                   /id="PRO_0000451887"
SQ   SEQUENCE   346 AA;  40508 MW;  B5FC0B322F19E890 CRC64;
     MSSFDYRSRL KELSARYNPE ASILVNERMQ SEDHYLDTDV VRYVKRSMRA VDDDYTKRTK
     DAGEAVKQHL NNELINVTYE YQGSVMTNTH IKGASDIDLL VICEKFEDTE INRVRDCLKT
     PYGYSNIQLS RLRNYELSFS LYRGDSREDL SNLRRQIESI MISKYTICDI SKAKSVRITN
     QHLHRDVDIV TSSWFQSLEY VLDGMPKEEK GIKIYNKNLG FAEGPDFPFL SISRINQKSS
     ESNGRLKRMI RFLKNVRTDS QKDIQLTSFD INAICYSIPV ADYAYLDYKQ LVYLLWSTMY
     HLWYDNKLDK LKSVVGDEYV FKGKPNKIEA LKALEDDVFK IHQDLN