ID A0A090W7E0_9FLAO Unreviewed; 261 AA.
AC A0A090W7E0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Diadenylate cyclase {ECO:0000256|HAMAP-Rule:MF_01499};
DE Short=DAC {ECO:0000256|HAMAP-Rule:MF_01499};
DE EC=2.7.7.85 {ECO:0000256|HAMAP-Rule:MF_01499};
DE AltName: Full=Cyclic-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_01499};
DE Short=c-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_01499};
GN Name=dacA {ECO:0000256|HAMAP-Rule:MF_01499};
GN ORFNames=CLV33_10863 {ECO:0000313|EMBL:PQV46909.1}, JCM19301_2614
GN {ECO:0000313|EMBL:GAL68891.1}, JCM19302_1774
GN {ECO:0000313|EMBL:GAL72925.1}, JCM19538_1065
GN {ECO:0000313|EMBL:GAL91007.1};
OS Jejuia pallidilutea.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Jejuia.
OX NCBI_TaxID=504487 {ECO:0000313|EMBL:GAL72925.1, ECO:0000313|Proteomes:UP000029646};
RN [1] {ECO:0000313|Proteomes:UP000029641, ECO:0000313|Proteomes:UP000029646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19301 {ECO:0000313|EMBL:GAL68891.1,
RC ECO:0000313|Proteomes:UP000029641}, JCM 19302
RC {ECO:0000313|EMBL:GAL72925.1}, JCM 19538 {ECO:0000313|EMBL:GAL91007.1,
RC ECO:0000313|Proteomes:UP000030184}, and JCM19302
RC {ECO:0000313|Proteomes:UP000029646};
RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA Sawabe T., Sawabe T.;
RT "Draft Genome Sequence of Marine Flavobacterium Jejuia pallidilutea Strain
RT 11shimoA1 and Pigmentation Mutants.";
RL Genome Announc. 2:e01236-14(2014).
RN [2] {ECO:0000313|EMBL:PQV46909.1, ECO:0000313|Proteomes:UP000251545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21165 {ECO:0000313|EMBL:PQV46909.1,
RC ECO:0000313|Proteomes:UP000251545};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (FEB-2018) 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_01499}.
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_01499};
CC -!- SUBUNIT: Probably a homodimer. {ECO:0000256|HAMAP-Rule:MF_01499}.
CC -!- SIMILARITY: Belongs to the adenylate cyclase family. DacA/CdaA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01499}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01499}.
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:GAL72925.1}.
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DR EMBL; BBNR01000027; GAL68891.1; -; Genomic_DNA.
DR EMBL; BBNS01000034; GAL72925.1; -; Genomic_DNA.
DR EMBL; BBNY01000090; GAL91007.1; -; Genomic_DNA.
DR EMBL; PVEO01000008; PQV46909.1; -; Genomic_DNA.
DR RefSeq; WP_042246549.1; NZ_PVEO01000008.1.
DR AlphaFoldDB; A0A090W7E0; -.
DR STRING; 504487.JCM19538_1065; -.
DR eggNOG; COG1624; Bacteria.
DR OrthoDB; 9807385at2; -.
DR Proteomes; UP000029641; Unassembled WGS sequence.
DR Proteomes; UP000029646; Unassembled WGS sequence.
DR Proteomes; UP000030184; Unassembled WGS sequence.
DR Proteomes; UP000251545; 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 HAMAP; MF_01499; DacA; 1.
DR InterPro; IPR014046; C-di-AMP_synthase.
DR InterPro; IPR034701; CdaA.
DR InterPro; IPR045585; CdaA_N.
DR InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR PANTHER; PTHR34185; DIADENYLATE CYCLASE; 1.
DR PANTHER; PTHR34185:SF1; DIADENYLATE CYCLASE; 1.
DR Pfam; PF19293; CdaA_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_01499};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01499};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01499};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01499};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01499};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01499};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01499};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01499}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT DOMAIN 82..249
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
SQ SEQUENCE 261 AA; 29459 MW; 745558F480272C56 CRC64;
MNIFDDILNL RFIDYLDVFL VALLLYYLYK LVKGTVAINI FLGIIIIYGA WKLTEFLNME
LLNGIFGGFM KVGIIALIVV FQPEIRKFLL MVGSTNFSRR RKFLKQFKFL KTEGTIATNV
DAIISACNKM SMSKTGALIV FERNNNLDFL SESGDEMNIK VTQPIIESIF FKNSPLHDGA
IIVSNNIVKA TRVILPVNND KNIPQRFGLR HRAAIGVTEK TDALALAVSE ETGHISYFKD
GEFVVFEDTT ELAKIIKKDL S
//
