ID A0A0M2PHF5_9BACI Unreviewed; 222 AA.
AC A0A0M2PHF5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=WQ54_19550 {ECO:0000313|EMBL:KKI90188.1};
OS Bacillus sp. SA1-12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI90188.1, ECO:0000313|Proteomes:UP000034887};
RN [1] {ECO:0000313|EMBL:KKI90188.1, ECO:0000313|Proteomes:UP000034887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1-12 {ECO:0000313|EMBL:KKI90188.1,
RC ECO:0000313|Proteomes:UP000034887};
RA Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) 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:KKI90188.1}.
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DR EMBL; LATZ01000119; KKI90188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2PHF5; -.
DR PATRIC; fig|1455638.3.peg.4296; -.
DR OrthoDB; 9807385at2; -.
DR Proteomes; UP000034887; 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; 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 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 50..209
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
SQ SEQUENCE 222 AA; 24768 MW; C3F737562F5D2024 CRC64;
MQRRVDQLEE SNPFTDIKNH ISFHLEQIIE EAELMRSSIG EKDYCLLCEL AHIRDRFNEI
QSSASFFYLK AYISDYTKNY IEIARAIQNL SDRRHGALLV IERNQVVGSL LQGGIQLNAN
LSSRLIESIF FPGNPLHDGA VLIKGDYIIS AANVLPLTEQ NFGNKKVGTR HRAAIGLSEV
TDALVLVVSE ETGKMSFALD GTLYPISSTD AGLQNGDILN KR
//
