DNCV2_ECOLX
ID DNCV2_ECOLX Reviewed; 432 AA.
AC P0DTF0;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=Cyclic GMP-AMP synthase {ECO:0000250|UniProtKB:Q9KVG7};
DE Short=c-GAMP synthase;
DE Short=c-GMP-AMP synthase;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:Q9KVG7};
DE AltName: Full=3'3'-cGAMP synthase {ECO:0000250|UniProtKB:Q9KVG7};
DE AltName: Full=Cyclic AMP-GMP synthase {ECO:0000250|UniProtKB:Q9KVG7};
DE Short=c-AMP-GMP synthase;
DE AltName: Full=Dinucleotide cyclase DncV {ECO:0000250|UniProtKB:Q9KVG7};
GN Name=dncV {ECO:0000303|PubMed:31533127}; ORFNames=ESG_RS0100135;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW11681;
RX PubMed=21078854; DOI=10.1128/iai.00932-10;
RA Sahl J.W., Steinsland H., Redman J.C., Angiuoli S.V., Nataro J.P.,
RA Sommerfelt H., Rasko D.A.;
RT "A comparative genomic analysis of diverse clonal types of enterotoxigenic
RT Escherichia coli reveals pathovar-specific conservation.";
RL Infect. Immun. 79:950-960(2011).
RN [2]
RP NOMENCLATURE, AND SIMILARITY.
RC STRAIN=TW11681;
RX PubMed=30787435; DOI=10.1038/s41586-019-0953-5;
RA Whiteley A.T., Eaglesham J.B., de Oliveira Mann C.C., Morehouse B.R.,
RA Lowey B., Nieminen E.A., Danilchanka O., King D.S., Lee A.S.Y.,
RA Mekalanos J.J., Kranzusch P.J.;
RT "Bacterial cGAS-like enzymes synthesize diverse nucleotide signals.";
RL Nature 567:194-199(2019).
RN [3]
RP ANTIVIRAL DEFENSE, NOMENCLATURE, OPERON STRUCTURE, AND MUTAGENESIS OF
RP 129-ASP--ASP-131.
RC STRAIN=TW11681;
RX PubMed=31533127; DOI=10.1038/s41586-019-1605-5;
RA Cohen D., Melamed S., Millman A., Shulman G., Oppenheimer-Shaanan Y.,
RA Kacen A., Doron S., Amitai G., Sorek R.;
RT "Cyclic GMP-AMP signalling protects bacteria against viral infection.";
RL Nature 574:691-695(2019).
RN [4]
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 II-A(GA) CBASS system (PubMed:32839535).
CC {ECO:0000269|PubMed:31533127, ECO:0000303|PubMed:32839535}.
CC -!- FUNCTION: Catalyzes the synthesis of 3'3'-cyclic GMP-AMP (3'3'-cGAMP)
CC from GTP and ATP, a second messenger in cell signal transduction. Is
CC also able to produce c-di-AMP and c-di-GMP from ATP and GTP. Controls
CC the activity of cGAMP-activated phospholipase CapV, a patatin-like
CC lipase that is a direct 3',3'-cGAMP receptor encoded in the dncV
CC operon. {ECO:0000250|UniProtKB:Q9KVG7}.
CC -!- FUNCTION: Protects E.coli against phage infection. When capV and dncV
CC are introduced in E.coli MG1655 there is 1000-fold protection against
CC phage P1; protection against other phage (T2, T4, T5, T6 and lambda-
CC vir) requires the 2 subsequent genes (cap2 and cap3).
CC {ECO:0000269|PubMed:31533127}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = 3',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:35647,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:71501; Evidence={ECO:0000250|UniProtKB:Q9KVG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35648;
CC Evidence={ECO:0000250|UniProtKB:Q9KVG7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9KVG7};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9KVG7};
CC -!- INDUCTION: Part of the CBASS operon consisting of capV-dncV-cap2-cap3.
CC {ECO:0000305|PubMed:31533127}.
CC -!- MISCELLANEOUS: The sequence of this protein is available under the NCBI
CC RefSeq accession WP_000558641.1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CD-NTase family. A02 subfamily.
CC {ECO:0000305|PubMed:30787435}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Small sacrifice - Issue 239
CC of September 2021;
CC URL="https://web.expasy.org/spotlight/back_issues/239/";
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DR EMBL; AELD01000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_000558641.1; NZ_VTME01000123.1.
DR AlphaFoldDB; P0DTF0; -.
DR SMR; P0DTF0; -.
DR GO; GO:0140701; F:3',3'-cyclic GMP-AMP synthase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antiviral defense; ATP-binding; GTP-binding; Magnesium; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW Transferase.
FT CHAIN 1..432
FT /note="Cyclic GMP-AMP synthase"
FT /id="PRO_0000451855"
FT BINDING 110..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9KVG7"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9KVG7"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9KVG7"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9KVG7"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9KVG7"
FT BINDING 255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9KVG7"
FT BINDING 283
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9KVG7"
FT BINDING 297
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9KVG7"
FT BINDING 344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9KVG7"
FT MUTAGEN 129..131
FT /note="DID->AIA: No longer defends against phage."
FT /evidence="ECO:0000269|PubMed:31533127"
SQ SEQUENCE 432 AA; 49317 MW; 34BEF450F90F5D4C CRC64;
MHWDLNNYYS NNMDGLISKL KLSKTESTKL KELRQIVRER TRDVFKEARA VAADVKKHTL
TLEGVRLKLG QTNVRYLSTA DQAEVARLIF EMDDDARNDF INLQPRFWTQ GSFQYDTLNK
PFQPGQEMDI DDGTYMPMTV FESEPRIGHT LLLLLVDTSL KSLEAENDGW RFEEKNTCGR
IKIPHEKTHI DVPMYAIPKN QFQTKQTAAD SAHILKSESI FESVALNRDS REAYLVESDK
VNLALREGAK RWSISDPKIV EDWFNDSCKR IGGHVRSICR FMKAWRDAQW DVGGPSSISL
MTAVVNILNR EEHNDSDLAG TMKLVAKLLP DEFNRGLESP DDTDTKLLFP AEWDQNVHQK
TIVETMKTLY EILVDAENAN TREDALHKMN EAFGKRVTNA QLITSIAAAP AFHVSPSREP
EPRKINKTMV SG
