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Database: UniProt
Entry: U9VQV2_9CYAN
LinkDB: U9VQV2_9CYAN
Original site: U9VQV2_9CYAN 
ID   U9VQV2_9CYAN            Unreviewed;       263 AA.
AC   U9VQV2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=N836_13870 {ECO:0000313|EMBL:ESA35059.1};
OS   Leptolyngbya sp. Heron Island J.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya group; Leptolyngbya.
OX   NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA35059.1, ECO:0000313|Proteomes:UP000017515};
RN   [1] {ECO:0000313|EMBL:ESA35059.1, ECO:0000313|Proteomes:UP000017515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Heron Island J {ECO:0000313|EMBL:ESA35059.1,
RC   ECO:0000313|Proteomes:UP000017515};
RX   PubMed=24503993;
RA   Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA   Fromme P.;
RT   "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT   Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL   Genome Announc. 2:e01166-e01113(2014).
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:ESA35059.1}.
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DR   EMBL; AWNH01000069; ESA35059.1; -; Genomic_DNA.
DR   AlphaFoldDB; U9VQV2; -.
DR   STRING; 1385935.N836_13870; -.
DR   PATRIC; fig|1385935.3.peg.4240; -.
DR   eggNOG; COG1624; Bacteria.
DR   Proteomes; UP000017515; 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; IPR036888; DNA_integrity_DisA_N_sf.
DR   InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR   NCBIfam; TIGR00159; diadenylate cyclase CdaA; 1.
DR   PANTHER; PTHR34185; DIADENYLATE CYCLASE; 1.
DR   PANTHER; PTHR34185:SF1; DIADENYLATE CYCLASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000017515};
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..30
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   DOMAIN          55..219
FT                   /note="DAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51794"
SQ   SEQUENCE   263 AA;  29268 MW;  97CCD9E796640615 CRC64;
     MLVVIGERRN LWMIRGLIVL MLAAVLSHVL RLSLLGFVLT NLSFGAAVAM ALMLQAEIRR
     FLELLGRGEL MQLFSSSRTP TSRPDGVIDE LVDAVRELSQ KRTGALMILE LGPPIDENDF
     SVPGVRLNAD LSKELIQTIF QTSTLLHDGA ILIRASRVVS AGVILPISER IASRQLGTRH
     RAAMGITERI DNCLCIVVSE ETGSISIAQR GRLNRPLTSN RLRELLQEQF TPAVESDTVA
     PELLNLGRRL TGFWKWTRQL VRR
//
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