CDNE_CAPGB
ID CDNE_CAPGB Reviewed; 351 AA.
AC A0A381HBN1;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=c-di-GMP synthase {ECO:0000303|PubMed:32877915};
DE EC=2.7.7.65 {ECO:0000269|PubMed:32877915};
DE AltName: Full=CgCdnE {ECO:0000303|PubMed:32877915};
DE AltName: Full=cGAS/DncV-like nucleotidyltransferase;
DE Short=CD-NTase;
GN Name=cdnE; ORFNames=NCTC12948_02564;
OS Capnocytophaga granulosa (strain ATCC 51502 / DSM 11449 / JCM 8566 / LMG
OS 16022 / NCTC 12948 / B0611).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=641143;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51502 / DSM 11449 / JCM 8566 / LMG 16022 / NCTC 12948 / B0611;
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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).
RN [3] {ECO:0007744|PDB:6WT9}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-351, FUNCTION, CATALYTIC
RP 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).
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. E05 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UFVE01000002; SUX93681.1; -; Genomic_DNA.
DR RefSeq; WP_016421262.1; NZ_KE150243.1.
DR PDB; 6WT9; X-ray; 2.30 A; A=2-351.
DR PDBsum; 6WT9; -.
DR AlphaFoldDB; A0A381HBN1; -.
DR SMR; A0A381HBN1; -.
DR STRING; 641143.HMPREF9331_02453; -.
DR EnsemblBacteria; SUX93681; SUX93681; NCTC12948_02564.
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 InterPro; IPR043519; NT_sf.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; GTP-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..351
FT /note="c-di-GMP synthase"
FT /id="PRO_0000451884"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:6WT9"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6WT9"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:6WT9"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:6WT9"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:6WT9"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:6WT9"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:6WT9"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:6WT9"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:6WT9"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:6WT9"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:6WT9"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 245..259
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 268..276
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:6WT9"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:6WT9"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 291..304
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 306..310
FT /evidence="ECO:0007829|PDB:6WT9"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 327..347
FT /evidence="ECO:0007829|PDB:6WT9"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:6WT9"
SQ SEQUENCE 351 AA; 41130 MW; 6D6EB81C2BFCCC2D CRC64;
MEKKNYSALF ENLQNRSNPE KLQEITTKFF SDNPDVKYND VLKYITLAMN GVSPEYTNKS
REAGEKVKLH LQDILLDVEY QYQGSVMTNT HIKGYSDIDL LVISDKFYTL DERNIIENLE
VNKFSLSQEK IQKLQQELLG KKYHSATNDL KNNRLLSEQK LSSVYEICDI THPKAIKITN
KSMGRDVDIV IANWYDDAQS VINNRQIEYR GIQIYNKRSN TIENRDFPFL SIQRINKRSS
ETKGRLKKMI RFLKNLKADS DEKIELSSFD INAICYNIEK NKYLHSNKYQ LVPILYEQLN
ELVSNSNKIN SLKSVDGHEY IFSRNNIDKK ESLKMLLQEV KIIYSNLQSY L
