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Database: UniProt
Entry: D1QSM3_9BACT
LinkDB: D1QSM3_9BACT
Original site: D1QSM3_9BACT 
ID   D1QSM3_9BACT            Unreviewed;       259 AA.
AC   D1QSM3;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=HMPREF0971_01982 {ECO:0000313|EMBL:EFB31704.1};
OS   Segatella oris F0302.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=649760 {ECO:0000313|EMBL:EFB31704.1, ECO:0000313|Proteomes:UP000004079};
RN   [1] {ECO:0000313|EMBL:EFB31704.1, ECO:0000313|Proteomes:UP000004079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0302 {ECO:0000313|EMBL:EFB31704.1,
RC   ECO:0000313|Proteomes:UP000004079};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2009) 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:EFB31704.1}.
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DR   EMBL; ACUZ02000034; EFB31704.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1QSM3; -.
DR   STRING; 649760.HMPREF0971_01982; -.
DR   HOGENOM; CLU_038561_0_0_10; -.
DR   Proteomes; UP000004079; 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        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   TRANSMEM        32..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   TRANSMEM        56..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   DOMAIN          79..247
FT                   /note="DAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51794"
SQ   SEQUENCE   259 AA;  29234 MW;  6C440BFA1030FAC0 CRC64;
     MMPFDFGIKD VIDIFLVALI LYYLYRLMKE SRSLNIFIGV MVFVLVWLFV SQVLEMRLLG
     SILDKLVGVG AIALIVLFQE EIRRFLYSLG AHQRIKQFSR FFGQRRDEKN REATRQMIMP
     IVLACMSMAK AKVGALIVIE RSAPLDDIVE TGDTIDANIN QRLIENIFFK NSPLHDGAMI
     ISRKRIKAAG CILPVSHNLD IPKELGLRHR AAMGISQDSD AVAIVVSEET GRISVAIRGQ
     FHLRLSAEEL ESILTSEID
//
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