CDNE_ECOLX
ID CDNE_ECOLX Reviewed; 297 AA.
AC Q6XGD5;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Cyclic UMP-AMP synthase {ECO:0000303|PubMed:30787435};
DE Short=cUMP-AMP synthase {ECO:0000303|PubMed:30787435};
DE EC=2.7.7.- {ECO:0000269|PubMed:30787435};
DE AltName: Full=3',3'-cUAMP synthase {ECO:0000305|PubMed:30787435};
DE AltName: Full=cGAS/DncV-like nucleotidyltransferase in E.coli {ECO:0000303|PubMed:30787435};
DE Short=CD-NTase056 {ECO:0000303|PubMed:30787435};
GN Name=cdnE {ECO:0000303|PubMed:30787435};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, NOMENCLATURE,
RP SIMILARITY, AND MUTAGENESIS OF 62-ASP--ASP-64.
RC STRAIN=ATCC 35350 / ECOR 31;
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 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(UA) CBASS system (PubMed:32839535).
CC {ECO:0000303|PubMed:32839535, ECO:0000305}.
CC -!- FUNCTION: Cyclic dinucleotide synthase that catalyzes the synthesis of
CC 3',3'-cyclic UMP-AMP (cUMP-AMP) from UTP and ATP, a second messenger
CC for cell signal transduction. Controls the activity of cUAMP-activated
CC phospholipase CapE, a patatin-like lipase that is a direct cUMP-AMP
CC receptor encoded in the cdnE operon. {ECO:0000269|PubMed:30787435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + UTP = 3',3'-cUAMP + 2 diphosphate; Xref=Rhea:RHEA:60456,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:143809; Evidence={ECO:0000269|PubMed:30787435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60457;
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.4. {ECO:0000269|PubMed:30787435};
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. E01 subfamily.
CC {ECO:0000305|PubMed:30787435}.
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DR EMBL; AY233333; AAP70312.1; -; Genomic_DNA.
DR RefSeq; WP_001593458.1; NZ_VTMJ01000059.1.
DR AlphaFoldDB; Q6XGD5; -.
DR SMR; Q6XGD5; -.
DR GO; GO:0005524; F:ATP 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 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; ATP-binding; Magnesium; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW Transferase.
FT CHAIN 1..297
FT /note="Cyclic UMP-AMP synthase"
FT /id="PRO_0000447700"
FT BINDING 48..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 48
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 64
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 174
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT BINDING 221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G2SLH8"
FT MUTAGEN 62..64
FT /note="DVD->AVA: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30787435"
SQ SEQUENCE 297 AA; 33796 MW; AB01F23A02C7E1B5 CRC64;
MGIPESQLDT WSHQGSIAQS ASTYSIIKNA LESANTKYHG KNFKVFLQGS YGNDTNIYAE
SDVDVVICLD DVYYSDLTQL SPEDKDAYDR AFVPATYSYT QFKQDVLEAL TERFGSDVKV
GDKAIVVAAN GSRRKADVIA SMQFRRYWKF KGHYDSQYDE GICFFNGAGE RIANYPKQHS
ENLTLKHQAS NKWLKPMVRV LKNLRSKLIA DGKLKSGLAP SYYLEGLLYN VPNEKFGTSY
ADCFVNAMNW IQTEADKDKL VCANEQYYLL WEGTHTSWEK ADAEAFIDAA IKMWNEW
