DNCV1_ECOLX
ID DNCV1_ECOLX Reviewed; 432 AA.
AC Q6XGD8;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Cyclic GMP-AMP synthase {ECO:0000303|PubMed:30837338};
DE Short=c-GAMP synthase {ECO:0000303|PubMed:30837338};
DE Short=c-GMP-AMP synthase;
DE EC=2.7.7.- {ECO:0000269|PubMed:30837338};
DE AltName: Full=3'3'-cGAMP synthase {ECO:0000303|PubMed:30837338};
DE AltName: Full=CD-NTase001 {ECO:0000303|PubMed:30787435};
GN Name=dncV {ECO:0000303|PubMed:25865248, ECO:0000303|PubMed:30837338};
GN ORFNames=DU321_04130 {ECO:0000312|EMBL:RRL50146.1};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000312|EMBL:AAP70298.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35350 / ECOR 31;
RX PubMed=14731283; DOI=10.1046/j.1365-2958.2003.03870.x;
RA Schubert S., Dufke S., Sorsa J., Heesemann J.;
RT "A novel integrative and conjugative element (ICE) of Escherichia coli: the
RT putative progenitor of the Yersinia high-pathogenicity island.";
RL Mol. Microbiol. 51:837-848(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB1727;
RA Garretto A., Miller-Ensminger T., Wolfe A.J., Putonti C.;
RT "E. coli isolates of the female bladder.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLN-110 AND 129-ASP--ASP-131.
RC STRAIN=ATCC 35350 / ECOR 31;
RX PubMed=30837338; DOI=10.1128/mbio.02492-18;
RA Li F., Cimdins A., Rohde M., Jaensch L., Kaever V., Nimtz M., Roemling U.;
RT "DncV Synthesizes Cyclic GMP-AMP and Regulates Biofilm Formation and
RT Motility in Escherichia coli ECOR31.";
RL MBio 10:0-0(2019).
RN [4]
RP NOMENCLATURE, AND SIMILARITY.
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 [5]
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 [6] {ECO:0007744|PDB:4XJ6}
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 1-407 IN COMPLEX WITH MAGNESIUM
RP AND 3'-DEOXY-GTP, AND COFACTOR.
RX PubMed=25865248; DOI=10.1016/j.str.2015.01.023;
RA Kato K., Ishii R., Hirano S., Ishitani R., Nureki O.;
RT "Structural basis for the catalytic mechanism of DncV, bacterial homolog of
RT cyclic GMP-AMP synthase.";
RL Structure 23:843-850(2015).
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-C(GA) CBASS system (PubMed:32839535).
CC {ECO:0000303|PubMed:32839535, ECO:0000305}.
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,
CC respectively; however, 3'3'-cGAMP is the dominant molecule produced by
CC DncV in vivo, contrary to the 2'3'-cGAMP produced by eukaryotes. By
CC producing cGAMP, down-regulates csgD expression and expression of
CC flagellum regulon genes, which leads to the down-regulation of rdar
CC biofilm formation and flagellum-mediated swimming and swarming motility
CC in a temperature-dependent manner (PubMed:30837338). Controls the
CC activity of cGAMP-activated phospholipase CapV, a patatin-like lipase
CC that is a direct 3',3'-cGAMP receptor encoded in the dncV operon (By
CC similarity). {ECO:0000250|UniProtKB:Q9KVG7,
CC ECO:0000269|PubMed:30837338}.
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:0000269|PubMed:30837338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35648;
CC Evidence={ECO:0000269|PubMed:30837338};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25865248};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:25865248};
CC -!- DISRUPTION PHENOTYPE: Deletion of dncV incrementally, but
CC significantly, enhances swimming and swarming motility compared to the
CC ECOR31 wild-type. It also enhances biofilm formation on abiotic
CC surfaces after 48 hours of development. {ECO:0000269|PubMed:30837338}.
CC -!- MISCELLANEOUS: This is a complex CBASS locus with the loci capE-cdnE-
CC probable diadenylate cyclase-capV-dcnV1-cap2-cap3.
CC {ECO:0000305|PubMed:14731283}.
CC -!- SIMILARITY: Belongs to the CD-NTase family. A01 subfamily.
CC {ECO:0000305|PubMed:30787435}.
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DR EMBL; AY233333; AAP70298.1; -; Genomic_DNA.
DR EMBL; RRVG01000003; RRL50146.1; -; Genomic_DNA.
DR RefSeq; WP_001593454.1; NZ_VTMJ01000059.1.
DR PDB; 4XJ6; X-ray; 2.31 A; A=1-407.
DR PDBsum; 4XJ6; -.
DR AlphaFoldDB; Q6XGD8; -.
DR SMR; Q6XGD8; -.
DR Proteomes; UP000272662; Unassembled WGS sequence.
DR GO; GO:0140701; F:3',3'-cyclic GMP-AMP synthase activity; IDA: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 3D-structure; Antiviral defense; ATP-binding; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide metabolism; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..432
FT /note="Cyclic GMP-AMP synthase"
FT /id="PRO_0000447705"
FT REGION 413..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25865248"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25865248,
FT ECO:0007744|PDB:4XJ6"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25865248,
FT ECO:0007744|PDB:4XJ6"
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 /evidence="ECO:0000269|PubMed:25865248,
FT ECO:0007744|PDB:4XJ6"
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:0000269|PubMed:25865248"
FT BINDING 297
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25865248"
FT BINDING 344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25865248"
FT MUTAGEN 110
FT /note="Q->A: Large decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:30837338"
FT MUTAGEN 129..131
FT /note="DID->AIA: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30837338"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:4XJ6"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 24..57
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:4XJ6"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:4XJ6"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4XJ6"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:4XJ6"
FT STRAND 128..138
FT /evidence="ECO:0007829|PDB:4XJ6"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 149..166
FT /evidence="ECO:0007829|PDB:4XJ6"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:4XJ6"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:4XJ6"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:4XJ6"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4XJ6"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4XJ6"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:4XJ6"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 274..289
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 318..335
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 357..377
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 382..393
FT /evidence="ECO:0007829|PDB:4XJ6"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:4XJ6"
SQ SEQUENCE 432 AA; 49276 MW; 84C0A7DCD253684E CRC64;
MPWDFNNYYS HNMDGLISKL KLSKTESDKL KALRQIVRER TRDVFQEARQ VAIDVRRQAL
TLESVRLKLE KTNVRYLSPE ERADLARLIF EMEDEARDDF IKFQPRFWTQ GSFQYDTLNR
PFHPGQEMDI DDGTYMPMTV FESEPSIGHT LLLLLVDTSL KSLEAENDGW VFEEKNTCGR
IKIYREKTHI DVPMYAIPKE QFQKKQTAAD SAHLIKSDSV FESFALNRGG REAYAVESDK
VNLALREGVR RWSVSDPKIV EDWFNESCKR IGGHLRSVCR FMKAWRDAQW EVGGPSSISL
MTAVVNILDR ESHNGSDLTG TMKLIARLLP EEFNRGVESP DDTDEKPLFP AESNHNVHHR
AIVETMEGLY GILLAAEQSE SREEALRKIN EAFGKRVTNA LLITSSAAAP AFLNAPSKEP
SSKPINKTMV SG
