CDNE_FLASX
ID CDNE_FLASX Reviewed; 365 AA.
AC P0DUE2;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 1.
DT 25-MAY-2022, entry version 5.
DE RecName: Full=c-di-GMP synthase {ECO:0000303|PubMed:32877915};
DE EC=2.7.7.65 {ECO:0000269|PubMed:32877915};
DE AltName: Full=FsCdnE {ECO:0000303|PubMed:32877915};
DE AltName: Full=cGAS/DncV-like nucleotidyltransferase;
DE Short=CD-NTase;
GN Name=cdnE {ECO:0000303|PubMed:32877915};
GN ORFNames=Ga0077528_101612, IMG 2624319774;
OS Flavobacteriaceae sp. genome_bin_11.
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2778089;
RN [1]
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).
RN [2] {ECO:0007744|PDB:6WT8}
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 2-365, FUNCTION, CATALYTIC
RP ACTIVITY, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF ASP-233.
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).
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 2624319774;
CC URL="https://img.jgi.doe.gov/cgi-bin/m/main.cgi?section=GeneDetail&page=genePageMainFaa&gene_oid=2624319774";
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DR PDB; 6WT8; X-ray; 2.80 A; A=2-365.
DR PDBsum; 6WT8; -.
DR AlphaFoldDB; P0DUE2; -.
DR SMR; P0DUE2; -.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; GTP-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..365
FT /note="c-di-GMP synthase"
FT /id="PRO_0000451886"
FT MUTAGEN 233
FT /note="D->A,N,S: Reduced efficiency of c-di-GMP synthesis,
FT makes small amounts of other cyclic-di-NMPs."
FT /evidence="ECO:0000269|PubMed:32877915"
FT HELIX 5..16
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 60..81
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6WT8"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:6WT8"
FT STRAND 106..117
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 154..172
FT /evidence="ECO:0007829|PDB:6WT8"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:6WT8"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:6WT8"
FT STRAND 193..204
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6WT8"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:6WT8"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:6WT8"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6WT8"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 300..314
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:6WT8"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:6WT8"
FT HELIX 336..360
FT /evidence="ECO:0007829|PDB:6WT8"
SQ SEQUENCE 365 AA; 42353 MW; B0EE657141FFA394 CRC64;
MQKNYLELIK KVRERSNPDL VQMTKMYSET LSGSKLFENK SIEYSDVSIY IKESMKGVAP
SYTMNSKVAA NKVEAHLKKS HGNLVDFERQ GSVMTNTHIL KENDVDLVQI TNKSSEFDHK
GLEKALNNTS VLKTEEILNL KKHKENFSPY QGNQIDDLKY VRLKSELVLS STYKTVDIEK
ENSIYVKVTE PERDIDVVTA TYYKSVDFMK TNDKSRKGIQ IYNKKTGKIN DVDYPFLSIE
RINVKDIISN RRLKNMIRFL KNIKYDCPHI ENKGSIRSFH INAICYNIDV KKYEDLHYLD
LVSILYQELT NIISNKSYRD NIKSVDGCEY IFEFDCAKKL IEIEFLSQEL DSIIADLHNQ
SLLVG
