CDNE2_LEGPN
ID CDNE2_LEGPN Reviewed; 295 AA.
AC P0DSP3;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Cyclic dipyrimidine nucleotide synthase {ECO:0000305|PubMed:30787435};
DE EC=2.7.7.- {ECO:0000269|PubMed:30787435};
DE AltName: Full=Cyclic CMP-UMP synthase {ECO:0000305|PubMed:30787435};
DE AltName: Full=c-di-UMP synthase {ECO:0000305|PubMed:30787435};
DE AltName: Full=cGAS/DncV-like nucleotidyltransferase {ECO:0000303|PubMed:30787435};
DE Short=CD-NTase057 {ECO:0000303|PubMed:30787435};
GN Name=cdnE02 {ECO:0000303|PubMed:30787435};
OS Legionella pneumophila.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=446;
RN [1]
RP FUNCTION, CATALYTIC ACTIVITY, NOMENCLATURE, AND SIMILARITY.
RC STRAIN=12_4117;
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 [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).
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 (Probable). A type I-B(UU) CBASS system (PubMed:32839535).
CC {ECO:0000303|PubMed:32839535, ECO:0000305,
CC ECO:0000305|PubMed:32839535}.
CC -!- FUNCTION: Cyclic dinucleotide synthase that catalyzes the synthesis of
CC 3',3'-cyclic UMP-UMP (c-di-UMP) as the major product, and of 3',3'-
CC cyclic CMP-UMP as a minor product, that are second messengers for cell
CC signal transduction. {ECO:0000269|PubMed:30787435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 UTP = c-di-UMP + 2 diphosphate; Xref=Rhea:RHEA:60480,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:143807;
CC Evidence={ECO:0000269|PubMed:30787435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60481;
CC Evidence={ECO:0000305|PubMed:30787435};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + UTP = cyclic CMP-UMP + 2 diphosphate;
CC Xref=Rhea:RHEA:60484, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:143811;
CC Evidence={ECO:0000269|PubMed:30787435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60485;
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 -!- SIMILARITY: Belongs to the CD-NTase family. E02 subfamily.
CC {ECO:0000305|PubMed:30787435}.
CC -!- CAUTION: The sequence of this protein is available under the NCBI
CC RefSeq accession WP_042646516, but the source is unknown.
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 RefSeq; WP_042646516.1; NZ_LAIX01000015.1.
DR AlphaFoldDB; P0DSP3; -.
DR SMR; P0DSP3; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide 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 CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR InterPro; IPR043519; NT_sf.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..295
FT /note="Cyclic dipyrimidine nucleotide synthase"
FT /id="PRO_0000447703"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
SQ SEQUENCE 295 AA; 33849 MW; 2C21757939EE2D89 CRC64;
MSIDWEQTFR KWSKPSSETE STKAENAERM IKAAINSSQI LSTKDISVFP QGSYRNNTNV
REDSDVDICV CLNTLVLSDY SLVPGMNDKL AELRTASYTY KQFKSDLETA LKNKFGTLGV
SRGDKAFDVH ANSYRVDADV VPAIQGRLYY DKNHNAFIRG TCIKPDSGGT IYNWPEQNYS
NGVNKNKSTG NRFKLIVRAI KRLRNHLAEK GYNTAKPIPS YLMECLVYIV PDQYFTGDSY
KTNVENCINY LYNQIDSSDW TEINEIKYLF GSHQMWNKTQ VKEFLLTAWS YIQKN
