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Database: UniProt
Entry: A0A0T5ZKS7_9CHLR
LinkDB: A0A0T5ZKS7_9CHLR
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ID   A0A0T5ZKS7_9CHLR        Unreviewed;       313 AA.
AC   A0A0T5ZKS7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=XU10_C0014G0046 {ECO:0000313|EMBL:KRT63189.1};
OS   Chloroflexi bacterium CSP1-4.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT63189.1, ECO:0000313|Proteomes:UP000051896};
RN   [1] {ECO:0000313|EMBL:KRT63189.1, ECO:0000313|Proteomes:UP000051896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT63189.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) 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:KRT63189.1}.
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DR   EMBL; LDXM01000014; KRT63189.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T5ZKS7; -.
DR   STRING; 1640513.XU10_C0014G0046; -.
DR   PATRIC; fig|1640513.3.peg.1414; -.
DR   Proteomes; UP000051896; 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; 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   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}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01499};
KW   Membrane {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}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_01499};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01499}.
FT   TRANSMEM        13..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   TRANSMEM        43..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   TRANSMEM        68..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT   DOMAIN          85..245
FT                   /note="DAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51794"
FT   REGION          284..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  33272 MW;  D5A22D2E96C89D93 CRC64;
     MDRILDTLTS LEIQPIAVVD IAITAVLIYW LFSLIRGTRA VRLVIGVISL YAVYVAAQAF
     GFQLLSQILQ TGAVVGLLAL VVVFQPELRR ALERIGRVGS LGWLWSGSHG EVQRVATEVS
     HAAALLSAER SGALIVLERE TGLEDAAETG VMLHADLSAE LLRTVFAPRA ALHDGAVLIR
     GAEIVAAGIV LPLAETTLQS ERLGTRHRAA LGITEQTDAV VVVVSEESGS IALVERARII
     RNLDEERLRT ALVSLLQPGG TRGRGVFTLP APGERGARAL RLVRRRGPGR HQPTATAPAP
     APRPAAVDGG KHG
//
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