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Database: UniProt
Entry: A0A124FLT8_9FIRM
LinkDB: A0A124FLT8_9FIRM
Original site: A0A124FLT8_9FIRM 
ID   A0A124FLT8_9FIRM        Unreviewed;       274 AA.
AC   A0A124FLT8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=XD69_0532 {ECO:0000313|EMBL:KUK41426.1};
OS   Clostridia bacterium 62_21.
OC   Bacteria; Bacillota; Clostridia.
OX   NCBI_TaxID=1635276 {ECO:0000313|EMBL:KUK41426.1, ECO:0000313|Proteomes:UP000067139};
RN   [1] {ECO:0000313|EMBL:KUK41426.1, ECO:0000313|Proteomes:UP000067139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=62_21 {ECO:0000313|EMBL:KUK41426.1};
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK41426.1}.
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DR   EMBL; LGFR01000038; KUK41426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124FLT8; -.
DR   PATRIC; fig|1635276.4.peg.1282; -.
DR   Proteomes; UP000067139; 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   NCBIfam; TIGR00159; diadenylate cyclase CdaA; 1.
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..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   TRANSMEM        38..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   DOMAIN          81..240
FT                   /note="DAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51794"
SQ   SEQUENCE   274 AA;  29537 MW;  8980D18B2F539D1E CRC64;
     MTLPALNSRL VLDILDILAI CLIGYMVVTV IRGTRAVQLL KGLLVLVALT GLAWWLELKL
     LSVVLDKVWT MAVVAIPIVF QPELRRMLER LGRGGSFTRL IVGQEAVNAA VGEVVQAVHE
     LAGKRTGALV AIERQTGLKE YIDTGVVLDA VVSRPLLVSI FEPHTPLHDG AVILRGNRVL
     AAGCYLPLSV SREIPSDLGT RHRAAVGLSE QSDAVVIVVS EETGVVSVAE DGVLRRGFDA
     EALAHYLQVR LATPHGFAWW VRARTGEGKK NAGV
//
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