ID T5HKL1_BACLI Unreviewed; 273 AA.
AC T5HKL1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=N399_00970 {ECO:0000313|EMBL:EQM25007.1};
OS Bacillus licheniformis CG-B52.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1368424 {ECO:0000313|EMBL:EQM25007.1, ECO:0000313|Proteomes:UP000017025};
RN [1] {ECO:0000313|Proteomes:UP000017025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG-B52 {ECO:0000313|Proteomes:UP000017025};
RA Galvez-Bobadilla E.J., Zarate-Bonilla L.J., Carrillo-Castro K., Guiza L.,
RA Pieper D.H., Salazar M., Junca H.;
RT "Draft genome of a Bacillus sp. strain CG-B52 virulent to shrimps.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQM25007.1, ECO:0000313|Proteomes:UP000017025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG-B52 {ECO:0000313|EMBL:EQM25007.1,
RC ECO:0000313|Proteomes:UP000017025};
RX PubMed=27174263;
RA Galvez E.J., Carrillo-Castro K., Zarate L., Guiza L., Pieper D.H.,
RA Garcia-Bonilla E., Salazar M., Junca H.;
RT "Draft Genome Sequence of Bacillus licheniformis CG-B52, a Highly Virulent
RT Bacterium of Pacific White Shrimp (Litopenaeus vannamei), Isolated from a
RT Colombian Caribbean Aquaculture Outbreak.";
RL Genome Announc. 4:0-0(2016).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01499};
CC Single-pass membrane protein {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: 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:EQM25007.1}.
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DR EMBL; AVEZ01000047; EQM25007.1; -; Genomic_DNA.
DR RefSeq; WP_003178443.1; NZ_AVEZ01000047.1.
DR AlphaFoldDB; T5HKL1; -.
DR GeneID; 66217653; -.
DR PATRIC; fig|1368424.3.peg.4487; -.
DR Proteomes; UP000017025; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 37..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01499"
FT DOMAIN 82..242
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
SQ SEQUENCE 273 AA; 30560 MW; 7D55BE4B22ACBDC9 CRC64;
MAFEDIPFLQ YLGDAVDILL VWYVIYKLMM VIRGTKAVQL LKGIVVIVLV RLASQYLGLS
TLQWLVDQAI TWGFLAIIII FQPELRRALE QLGRGRFFSR SGTPEEEQQQ KTIDAITKAI
KYMAKRRIGA LLTIERETGM GDYIETGIPL NAKVSSELLI NIFIPNTPLH DGAVIMKNDE
VAAAACYLPL SESPFISKEL GTRHRAAVGI SEVTDSLTVV VSEETGGISV AKNGDLHRDL
SEEALKNMLE AEFKKNSRET SSNRWYWRAK KNG
//
