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Database: UniProt
Entry: G7MB89_9CLOT
LinkDB: G7MB89_9CLOT
Original site: G7MB89_9CLOT 
ID   G7MB89_9CLOT            Unreviewed;       283 AA.
AC   G7MB89;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=CDLVIII_0476 {ECO:0000313|EMBL:EHI97211.1};
OS   Clostridium sp. DL-VIII.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI97211.1, ECO:0000313|Proteomes:UP000005106};
RN   [1] {ECO:0000313|EMBL:EHI97211.1, ECO:0000313|Proteomes:UP000005106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DL-VIII {ECO:0000313|EMBL:EHI97211.1,
RC   ECO:0000313|Proteomes:UP000005106};
RX   PubMed=23929491;
RA   Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT   Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL   Genome Announc. 1:e00605-e00613(2013).
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}.
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DR   EMBL; CM001240; EHI97211.1; -; Genomic_DNA.
DR   RefSeq; WP_009167893.1; NZ_CM001240.1.
DR   AlphaFoldDB; G7MB89; -.
DR   STRING; 641107.CDLVIII_0476; -.
DR   eggNOG; COG1624; Bacteria.
DR   HOGENOM; CLU_038561_0_1_9; -.
DR   Proteomes; UP000005106; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000005106};
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        15..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   TRANSMEM        45..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   DOMAIN          87..247
FT                   /note="DAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51794"
SQ   SEQUENCE   283 AA;  31636 MW;  6B1D4FCF3C12A8EF CRC64;
     MNELLSMLVQ SFSNMSIWSV LDILVVSFIF YKGYMLIKET RAEQLLKGIL LIIALIPISY
     LLRLDMLYFI LNKTLTIGVL SVIIIFQPEI RRALEHLGRS AFDDKHYQNN KEAFNSTINE
     IATAVQNLSE SKTGALIVIE QSTGLNEIIG QGTLLDANVT SNLLENIFVV NTPLHDGATI
     IRNNRILASG CVLPLTDNNT ISKKLGTRHR AAMGLSEVSD ALVVIVSEET GVISLAINGR
     ITRGYDKDRL KIVLTKIIEN RNEKKVKSAG ERVRSWIRVK TER
//
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