DACZ_METJA
ID DACZ_METJA Reviewed; 309 AA.
AC Q58408;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Diadenylate cyclase {ECO:0000255|HAMAP-Rule:MF_00840};
DE Short=DAC {ECO:0000255|HAMAP-Rule:MF_00840};
DE EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_00840};
DE AltName: Full=Cyclic-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00840};
DE Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00840};
DE AltName: Full=Diadenylyl cyclase {ECO:0000303|PubMed:23812326};
GN Name=dacZ {ECO:0000255|HAMAP-Rule:MF_00840, ECO:0000303|PubMed:23812326};
GN Synonyms=dacY {ECO:0000303|PubMed:23812326}; OrderedLocusNames=MJ1002;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP GENE NAME.
RX PubMed=23812326; DOI=10.1038/nrmicro3069;
RA Corrigan R.M., Gruendling A.;
RT "Cyclic di-AMP: another second messenger enters the fray.";
RL Nat. Rev. Microbiol. 11:513-524(2013).
RN [3]
RP FUNCTION, AND EXPRESSION IN E.COLI.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=25965978; DOI=10.1021/jacs.5b00275;
RA Kellenberger C.A., Chen C., Whiteley A.T., Portnoy D.A., Hammond M.C.;
RT "RNA-based fluorescent biosensors for live cell imaging of second messenger
RT cyclic di-AMP.";
RL J. Am. Chem. Soc. 137:6432-6435(2015).
CC -!- FUNCTION: Diadenylate cyclase that catalyzes the condensation of 2 ATP
CC molecules into cyclic di-AMP (c-di-AMP) (PubMed:25965978). c-di-AMP is
CC a second messenger for intracellular signal transduction involved in
CC the control of important regulatory processes such as osmoregulation
CC (By similarity). {ECO:0000255|HAMAP-Rule:MF_00840,
CC ECO:0000305|PubMed:25965978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00840};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00840};
CC -!- SIMILARITY: Belongs to the adenylate cyclase family. DacZ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00840}.
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DR EMBL; L77117; AAB99005.1; -; Genomic_DNA.
DR PIR; A64425; A64425.
DR RefSeq; WP_010870515.1; NC_000909.1.
DR AlphaFoldDB; Q58408; -.
DR SMR; Q58408; -.
DR STRING; 243232.MJ_1002; -.
DR EnsemblBacteria; AAB99005; AAB99005; MJ_1002.
DR GeneID; 1451899; -.
DR KEGG; mja:MJ_1002; -.
DR eggNOG; arCOG04453; Archaea.
DR HOGENOM; CLU_063222_2_0_2; -.
DR InParanoid; Q58408; -.
DR OMA; GHESFIF; -.
DR OrthoDB; 80301at2157; -.
DR PhylomeDB; Q58408; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106408; F:diadenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019932; P:second-messenger-mediated signaling; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1380.20; -; 1.
DR Gene3D; 3.40.1700.10; -; 1.
DR HAMAP; MF_00840; DacZ; 1.
DR InterPro; IPR014499; DAC_DacZ.
DR InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR Pfam; PF02457; DAC; 1.
DR Pfam; PF02887; PK_C; 1.
DR PIRSF; PIRSF019073; UCP019073; 1.
DR SUPFAM; SSF143597; SSF143597; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR PROSITE; PS51794; DAC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Manganese; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="Diadenylate cyclase"
FT /id="PRO_0000107138"
FT DOMAIN 144..301
FT /note="DAC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00840"
SQ SEQUENCE 309 AA; 34380 MW; 382D44A261C76907 CRC64;
MIAKYIIKHG LELAYDIKAD AFMIFTETGK SYELLKSFLK KDEHSGIIKI LDKISHKNVK
IIVATPNQVT YKKISSENEE NIYPIFIKHR EDNRCMIISS GIVHALKMKI LKENNKIVAV
VGEPKTPGKL DTIMVVNVKE HVKTITLYEL FETLDEKQKR TLKEIIKLAM EIGREGREGE
YVGTIFVMGD TLNVMSMSKP LILNPFAGHN ASIFDENVKG TIKELSSIDG AFIITDEGKV
VSAGRFLEIK GDVNIPKGLG ARHLAAASIS KNTNAIAVTV SQSGGIVRVF KDGKIVFETD
PRANILFFD
