ID R0N447_STRMT Unreviewed; 285 AA.
AC R0N447;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=D064_07990 {ECO:0000313|EMBL:EOB21230.1};
OS Streptococcus mitis 11/5.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1239792 {ECO:0000313|EMBL:EOB21230.1, ECO:0000313|Proteomes:UP000013365};
RN [1] {ECO:0000313|EMBL:EOB21230.1, ECO:0000313|Proteomes:UP000013365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11/5 {ECO:0000313|EMBL:EOB21230.1,
RC ECO:0000313|Proteomes:UP000013365};
RA Ikryannikova L.N., Ilina E.N., Kostryukova E.S., Semashko T.A.,
RA Karpova I.Y.U., Larin A.K., Ischenko D.S., Alekseev D.G., Klimova E.A.,
RA Filimonova A.V., Savinova T.A., Filimonova O.Y.U., Dubovickaya V.A.,
RA Sidorenko S.V., Govorun V.M.;
RL Submitted (APR-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:EOB21230.1}.
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DR EMBL; AQTT01000022; EOB21230.1; -; Genomic_DNA.
DR AlphaFoldDB; R0N447; -.
DR PATRIC; fig|1239792.3.peg.1562; -.
DR Proteomes; UP000013365; 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 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT TRANSMEM 49..67
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT TRANSMEM 73..92
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT DOMAIN 93..253
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
SQ SEQUENCE 285 AA; 31777 MW; 2F23E0D1F71F6366 CRC64;
MNFQQLSNLQ YWTSLFSSPW SIAINLFDIL IVAYILYRFT KAIAGTKIMI LVRGVVIFVL
AQVVANILDL TTISWLINQI ITYGVIAAVV IFSPEIRTGL ERLGRATDFF STAQISAEEQ
MIRAFVKSVE YMSPRKIGAL VAIQRVRTLQ EYIATGIPLD ANISAELLIN IFIPNTPLHD
GAVIIRENRI AVTSAYLPLT ESTGISKEFG TRHRAAIGLS EVSDALTFIV SEETGGISIT
YNGVFKHDLT IEEFEAELRA ILLPAVEEKV SFKDRLLGGW KYEKK
//
