ID U5DCR4_9CHRO Unreviewed; 304 AA.
AC U5DCR4;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, 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=KR51_00010050 {ECO:0000313|EMBL:ERN42318.1};
OS Rubidibacter lacunae KORDI 51-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rubidibacter.
OX NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN42318.1, ECO:0000313|Proteomes:UP000016960};
RN [1] {ECO:0000313|EMBL:ERN42318.1, ECO:0000313|Proteomes:UP000016960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN42318.1,
RC ECO:0000313|Proteomes:UP000016960};
RA Choi D.H., Noh J.H., Kwon K.-K., Lee J.-H., Ryu J.-Y.;
RT "Draft genome sequence of Rubidibacter lacunae KORDI 51-2.";
RL Submitted (MAY-2013) 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:ERN42318.1}.
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DR EMBL; ASSJ01000026; ERN42318.1; -; Genomic_DNA.
DR RefSeq; WP_022605289.1; NZ_ASSJ01000026.1.
DR AlphaFoldDB; U5DCR4; -.
DR STRING; 582515.KR51_00010050; -.
DR PATRIC; fig|582515.4.peg.1121; -.
DR eggNOG; COG1624; Bacteria.
DR InParanoid; U5DCR4; -.
DR OrthoDB; 9807385at2; -.
DR Proteomes; UP000016960; 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:UP000016960};
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..36
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT TRANSMEM 43..61
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT DOMAIN 90..254
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
SQ SEQUENCE 304 AA; 32876 MW; 367A468CE01D0C10 CRC64;
MPPSGSADTT SFAVWFFFAL DIGLVTILAF LLLLAIGERS TLWIVRGLLL MLVLLLLGFI
GSNFLGLTIL PFVLEKAIVG LTVAAALIFQ AELRQFLEFL GRGELWQWMQ ASRRTPTGAS
DVIGEIVDAV KDLSQNRIGA LIVVETGGAF EPHAFSDPGV PLNAEISTEL LQTIFQTTTL
LHDGAVLIRG SRIAAAGVIL PITEKVLSRQ LGTRHRAAIG ITERSANCLC IVVSEETGSI
SLAERGNLNR PLTRGKLEEL LALRFTPAVE LESVAPGLGR LSRQGQALLE RLLRLLPPTS
HEKK
//
