CDND2_ENTCL
ID CDND2_ENTCL Reviewed; 381 AA.
AC P0DSP4;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=Cyclic AMP-AMP-GMP synthase {ECO:0000305|PubMed:30787435};
DE EC=2.7.7.- {ECO:0000269|PubMed:30787435};
DE AltName: Full=cGAS/DncV-like nucleotidyltransferase {ECO:0000303|PubMed:30787435};
DE Short=CD-NTase038 {ECO:0000303|PubMed:30787435};
GN Name=cdnD02 {ECO:0000303|PubMed:30787435};
GN ORFNames=P853_02262 {ECO:0000312|EMBL:EUL38999.1};
OS Enterobacter cloacae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCI 50;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Murphy C., Cosimi L., Cerqueira G., Feldgarden M., Earl A., Hung D.,
RA Onderdonk A.B., Ferraro M.J., Hooper D., Dekker J., O'Brien T., Huang S.,
RA Quan V., Ernst C., Delaney M., DuBois A., Kim D.S., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterobacter cloacae UCI 50.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, NOMENCLATURE, AND SIMILARITY.
RC STRAIN=UCI 50;
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, OPERON STRUCTURE, AND MUTAGENESIS OF 69-ASP--ASP-71.
RC STRAIN=UCI 50;
RX PubMed=32544385; DOI=10.1016/j.cell.2020.05.019;
RA Lowey B., Whiteley A.T., Keszei A.F.A., Morehouse B.R., Antine S.P.,
RA Cabrera V.J., Kashin D., Schwede F., Mekalanos J.J., Shao S., Lee A.S.Y.,
RA Kranzusch P.J.;
RT "CBASS immunity uses CARF-related effectors to sense 3'-5' and 2'-5'-linked
RT cyclic oligonucleotide signals and protect bacteria from phage infection.";
RL Cell 182:38-49(2020).
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-C(AAG) CBASS system (PubMed:32839535).
CC {ECO:0000269|PubMed:32544385, ECO:0000303|PubMed:32839535}.
CC -!- FUNCTION: Cyclic trinucleotide synthase that catalyzes the synthesis of
CC 3',3',3'-cyclic AMP-AMP-GMP as the major product, a second messenger
CC for cell signal transduction. {ECO:0000269|PubMed:30787435}.
CC -!- FUNCTION: Protects E.coli against phage T2 infection. When the cdnD-
CC cap2-cap3-cap4 operon is introduced in E.coli there is a more than
CC 10(3) decrease in the efficiency of T2 plaque formation. The operon
CC does not protect against phage T5 and only about 10-fold against T7.
CC {ECO:0000269|PubMed:32544385}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + GTP = cyclic AMP-AMP-GMP + 3 diphosphate;
CC Xref=Rhea:RHEA:60476, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:143810;
CC Evidence={ECO:0000269|PubMed:30787435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60477;
CC Evidence={ECO:0000305|PubMed:30787435};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:G2SLH8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:G2SLH8};
CC -!- INDUCTION: Part of the CBASS operon consisting of cap4-cdnD-cap2-cap3.
CC {ECO:0000305|PubMed:32544385}.
CC -!- SIMILARITY: Belongs to the CD-NTase family. D02 subfamily.
CC {ECO:0000305|PubMed:30787435}.
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DR EMBL; JCKK01000002; EUL38999.1; -; Genomic_DNA.
DR PDB; 7D48; X-ray; 2.15 A; A=1-381.
DR PDB; 7D4J; X-ray; 2.09 A; A=1-381.
DR PDB; 7D4O; X-ray; 1.87 A; A/B=1-381.
DR PDB; 7D4S; X-ray; 1.93 A; A=1-381.
DR PDB; 7D4U; X-ray; 2.70 A; A=1-381.
DR PDB; 7LJL; X-ray; 1.45 A; A/B=1-381.
DR PDBsum; 7D48; -.
DR PDBsum; 7D4J; -.
DR PDBsum; 7D4O; -.
DR PDBsum; 7D4S; -.
DR PDBsum; 7D4U; -.
DR PDBsum; 7LJL; -.
DR AlphaFoldDB; P0DSP4; -.
DR SMR; P0DSP4; -.
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:0016779; F:nucleotidyltransferase activity; 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.
DR InterPro; IPR043519; NT_sf.
DR SUPFAM; SSF81301; SSF81301; 1.
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..381
FT /note="Cyclic AMP-AMP-GMP synthase"
FT /id="PRO_0000447704"
FT REGION 348..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT MUTAGEN 69..71
FT /note="DVD->AVA: No longer protects against phage T2."
FT /evidence="ECO:0000269|PubMed:32544385"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 18..37
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:7LJL"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:7LJL"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:7LJL"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:7LJL"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:7LJL"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:7LJL"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:7LJL"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:7LJL"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:7LJL"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:7LJL"
FT STRAND 197..205
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:7LJL"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 267..281
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:7LJL"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:7LJL"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 310..332
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 336..347
FT /evidence="ECO:0007829|PDB:7LJL"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:7LJL"
SQ SEQUENCE 381 AA; 43256 MW; 7FF5909D6F0B7470 CRC64;
MELQPQFNEF LANIRPTDTQ KEDWKSGART LRERLKNFEP LKEIVVSTFL QGSIRRSTAI
RPLGDKRPDV DIVVVTNLDH TRMSPTDAMD LFIPFLEKYY PGKWETQGRS FGITLSYVEL
DLVITAIPES GAEKSHLEQL YKSESVLTVN SLEEQTDWRL NKSWTPNTGW LSESNSAQVE
DAPASEWKAH PLVLPDREKN EWGRTHPLAQ IRWTAEKNRL CNGHYINLVR AVKWWRQQNS
EDLPKYPKGY PLEHLIGNAL DNGTTSMAQG LVQLMDTFLS RWAAIYNQKS KPWLSDHGVA
EHDVMARLTA EDFCSFYEGI ASAAEIARNA LASEEPQESA QLWRQLFGSK FPLPGPQGGD
RNGGFTTPSK PAEPQKTGRF A
