ID J7T9A2_BACCE Unreviewed; 201 AA.
AC J7T9A2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Diadenylate cyclase {ECO:0000256|HAMAP-Rule:MF_00838};
DE Short=DAC {ECO:0000256|HAMAP-Rule:MF_00838};
DE EC=2.7.7.85 {ECO:0000256|HAMAP-Rule:MF_00838};
DE AltName: Full=Cyclic-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_00838};
DE Short=c-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_00838};
GN Name=dacB {ECO:0000256|HAMAP-Rule:MF_00838};
GN ORFNames=IC3_04024 {ECO:0000313|EMBL:EJP87342.1};
OS Bacillus cereus VD142.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=718224 {ECO:0000313|EMBL:EJP87342.1, ECO:0000313|Proteomes:UP000006969};
RN [1] {ECO:0000313|EMBL:EJP87342.1, ECO:0000313|Proteomes:UP000006969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VD142 {ECO:0000313|EMBL:EJP87342.1,
RC ECO:0000313|Proteomes:UP000006969};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus VD142.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of 2 ATP molecules into cyclic di-
CC AMP (c-di-AMP), a second messenger used to regulate differing processes
CC in different bacteria. {ECO:0000256|HAMAP-Rule:MF_00838}.
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:0000256|ARBA:ARBA00000877, ECO:0000256|HAMAP-
CC Rule:MF_00838};
CC -!- SUBUNIT: Probably oligomerizes. {ECO:0000256|HAMAP-Rule:MF_00838}.
CC -!- SIMILARITY: Belongs to the adenylate cyclase family. DacB/CdaS
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00838}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJP87342.1}.
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DR EMBL; AHCL02000029; EJP87342.1; -; Genomic_DNA.
DR RefSeq; WP_002067925.1; NZ_KE150047.1.
DR AlphaFoldDB; J7T9A2; -.
DR GeneID; 66265512; -.
DR PATRIC; fig|718224.3.peg.4115; -.
DR HOGENOM; CLU_116655_0_0_9; -.
DR Proteomes; UP000006969; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106408; F:diadenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:InterPro.
DR GO; GO:0019932; P:second-messenger-mediated signaling; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1700.10; DNA integrity scanning protein, DisA, N-terminal domain; 1.
DR Gene3D; 1.10.287.770; YojJ-like; 1.
DR HAMAP; MF_00838; DacB; 1.
DR InterPro; IPR014046; C-di-AMP_synthase.
DR InterPro; IPR034693; CdaS.
DR InterPro; IPR019457; CdaS_N.
DR InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR NCBIfam; NF038328; c-di-AMP_CdaS; 1.
DR PANTHER; PTHR34185:SF2; CYCLIC DI-AMP SYNTHASE CDAS; 1.
DR PANTHER; PTHR34185; DIADENYLATE CYCLASE; 1.
DR Pfam; PF10372; CdaS_N; 1.
DR Pfam; PF02457; DAC; 1.
DR PIRSF; PIRSF004793; UCP004793; 1.
DR SUPFAM; SSF143597; YojJ-like; 1.
DR PROSITE; PS51794; DAC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00838}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_00838};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00838};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00838};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00838};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00838}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00838};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00838}.
FT DOMAIN 54..201
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
SQ SEQUENCE 201 AA; 22254 MW; CAD40D84F65FA931 CRC64;
MQEWGLSEEL KIKTKQMIEI AEKELSNMKH AIDKEDECIL CKMEDIHHML TNVQTLAATY
YIQAYLSPYT ESSHFITTAV QHLSARKHGA LIIVERSDAL DSFIQTGTTL NAHLTAPLLE
SIFYPGNPLH DGAVLIKNNH IVSAANILPL TKSMEINPEL GTRHRAAIGL SEKIDALILV
VSEETGRTSF ALGGTLYTIS L
//
