ID J8E5U5_BACCE Unreviewed; 216 AA.
AC J8E5U5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=IGC_00588 {ECO:0000313|EMBL:EJQ86747.1};
OS Bacillus cereus HuA4-10.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1053206 {ECO:0000313|EMBL:EJQ86747.1, ECO:0000313|Proteomes:UP000006977};
RN [1] {ECO:0000313|EMBL:EJQ86747.1, ECO:0000313|Proteomes:UP000006977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HuA4-10 {ECO:0000313|EMBL:EJQ86747.1,
RC ECO:0000313|Proteomes:UP000006977};
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., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus HuA4-10.";
RL Submitted (APR-2012) 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:EJQ86747.1}.
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 EMBL; AHEA01000004; EJQ86747.1; -; Genomic_DNA.
DR AlphaFoldDB; J8E5U5; -.
DR PATRIC; fig|1053206.3.peg.604; -.
DR HOGENOM; CLU_116655_0_0_9; -.
DR Proteomes; UP000006977; 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 69..216
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
SQ SEQUENCE 216 AA; 24112 MW; 360F681A7B5F9A82 CRC64;
MYTLWLNTPP KGMRIMQEWG LSEELKIKTK QMIEIAEKEL SNMKHAIDKE DECILCKMED
IHHMLTNVQT LAATYYIQAY LSPYTESSHF ITAAVQHLSA RKHGALIVVE RNETLESFIQ
IGTTLNAHLT APLLESIFYP GNPLHDGAVL IKNNHIVSAA NILPLTKSTE IDPELGTRHR
AAIGLSEKSD ALILVVSEET GRTSFALNGT LYTISL
//
