ID A0A136WIG3_9FIRM Unreviewed; 284 AA.
AC A0A136WIG3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-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=disA_2 {ECO:0000313|EMBL:KXL54332.1};
GN Synonyms=dacA {ECO:0000256|HAMAP-Rule:MF_01499}, disA_1
GN {ECO:0000313|EMBL:KXL54207.1};
GN ORFNames=CLNEO_03080 {ECO:0000313|EMBL:KXL54207.1}, CLNEO_04370
GN {ECO:0000313|EMBL:KXL54332.1};
OS Anaerotignum neopropionicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerotignum.
OX NCBI_TaxID=36847 {ECO:0000313|EMBL:KXL54332.1, ECO:0000313|Proteomes:UP000070539};
RN [1] {ECO:0000313|EMBL:KXL54332.1, ECO:0000313|Proteomes:UP000070539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM-3847 {ECO:0000313|EMBL:KXL54332.1,
RC ECO:0000313|Proteomes:UP000070539};
RA Poehlein A., Beck M.H., Bengelsdorf F.R., Daniel R., Duerre P.;
RT "Genome sequence of Clostridium neopropionicum X4, DSM-3847.";
RL Submitted (JAN-2016) 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:KXL54332.1}.
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DR EMBL; LRVM01000001; KXL54207.1; -; Genomic_DNA.
DR EMBL; LRVM01000001; KXL54332.1; -; Genomic_DNA.
DR RefSeq; WP_066083790.1; NZ_LRVM01000001.1.
DR AlphaFoldDB; A0A136WIG3; -.
DR STRING; 36847.CLNEO_03080; -.
DR PATRIC; fig|36847.3.peg.383; -.
DR OrthoDB; 9807385at2; -.
DR Proteomes; UP000070539; 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}; Reference proteome {ECO:0000313|Proteomes:UP000070539};
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..257
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
SQ SEQUENCE 284 AA; 31512 MW; CEC3B09AB8C540F0 CRC64;
MESIKGFFDN LGVTGFVRPS IGFSDFLDIL IVAYIIYKII FWIKETRAWV LFKGILVILG
LAAIATILQL NTILWILSNT ISVGIIAVIV VFQPELRKAL EQLGKGQFFS YFIRNEEEDN
QKASARTVDE IIKAVDKMGA VRTGALILIE QEVPLGDLER TGIPIDAVIS SQLLINIFEH
NTPLHDGAVI VRRNRVAAAT CFLPLTDSNE VSMELGTRHR AAIGASEVSD AYVIVVSEET
GSISVARGGV LYRDLTMEQL RTMLSQTKKV GKKKLSFWKG RQDK
//
