CDAS_BACT1
ID CDAS_BACT1 Reviewed; 201 AA.
AC D5TM67;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Diadenylate cyclase CdaS {ECO:0000303|PubMed:26441857};
DE Short=DAC {ECO:0000255|HAMAP-Rule:MF_00838};
DE EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_00838, ECO:0000269|PubMed:26441857};
DE AltName: Full=Cyclic-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00838};
DE Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00838};
GN Name=cdaS {ECO:0000303|PubMed:26441857}; Synonyms=dacB;
GN OrderedLocusNames=BMB171_C4535;
OS Bacillus thuringiensis (strain BMB171).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=714359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMB171;
RX PubMed=20525827; DOI=10.1128/jb.00562-10;
RA He J., Shao X., Zheng H., Li M., Wang J., Zhang Q., Li L., Liu Z., Sun M.,
RA Wang S., Yu Z.;
RT "Complete genome sequence of Bacillus thuringiensis mutant strain BMB171.";
RL J. Bacteriol. 192:4074-4075(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, DEVELOPMENTAL STAGE, INDUCTION, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF TRP-4; 131-ASP-GLY-132 AND 163-ARG--ARG-165.
RC STRAIN=BMB171;
RX PubMed=26441857; DOI=10.3389/fmicb.2015.00908;
RA Zheng C., Ma Y., Wang X., Xie Y., Ali M.K., He J.;
RT "Functional analysis of the sporulation-specific diadenylate cyclase CdaS
RT in Bacillus thuringiensis.";
RL Front. Microbiol. 6:908-908(2015).
CC -!- FUNCTION: One of 3 paralogous diadenylate cyclases (DAC) in this
CC bacteria catalyzing the condensation of 2 ATP molecules into cyclic di-
CC AMP (c-di-AMP). It has slow DAC activity with ADP as a substrate and
CC may have weak ADPase activity (PubMed:26441857). Required for efficient
CC spore formation, whereas in B.subtilis, it is required for efficient
CC spore germination. It is produced under the control of different sigma
CC factors in the two bacteria. It is also required for parasporal crystal
CC formation (PubMed:26441857). {ECO:0000269|PubMed:26441857}.
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:0000255|HAMAP-Rule:MF_00838,
CC ECO:0000269|PubMed:26441857};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:26441857};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:26441857};
CC -!- SUBUNIT: Probably forms a homohexamer (PubMed:26441857).
CC {ECO:0000305|PubMed:26441857}.
CC -!- DEVELOPMENTAL STAGE: Probably expressed only during sporulation.
CC {ECO:0000305|PubMed:26441857}.
CC -!- INDUCTION: First expressed at onset of sporulation, maximal
CC transcription at 18 hours during sporulation in mid-stationary phase.
CC Under control of sigma-H factor; in B.subtilis is under control of the
CC sigma-G factor. {ECO:0000269|PubMed:26441857}.
CC -!- DOMAIN: The N-terminal region (residues 1-69) is required for activity,
CC unlike the B.subtilis ortholog where their removal increases c-di-AMP
CC production. {ECO:0000269|PubMed:26441857}.
CC -!- DISRUPTION PHENOTYPE: Spore formation delayed by about 2 hours, about
CC 20-fold decrease in spore formation; 2-fold decrease in parasporal
CC crystal formation, 30% decreased c-di-AMP levels at 18 hours growth.
CC Double cdaS-disA and cdaS-cdaA mutants are viable, but neither double
CC cdaA-disA nor triple cdaA-cdaS-disA mutants can be made, suggesting c-
CC di-AMP is essential. {ECO:0000269|PubMed:26441857}.
CC -!- MISCELLANEOUS: This strain no longer produces parasporal crystals, but
CC can be made to do so upon transformation with appropriate plasmids.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the adenylate cyclase family. DacB/CdaS
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00838}.
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DR EMBL; CP001903; ADH09343.1; -; Genomic_DNA.
DR RefSeq; WP_000545252.1; NC_014171.1.
DR AlphaFoldDB; D5TM67; -.
DR SMR; D5TM67; -.
DR GeneID; 67509567; -.
DR KEGG; btb:BMB171_C4535; -.
DR HOGENOM; CLU_116655_0_0_9; -.
DR OMA; YYLRHYL; -.
DR OrthoDB; 1300262at2; -.
DR BRENDA; 2.7.7.85; 711.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
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 GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1700.10; -; 1.
DR HAMAP; MF_00838; DacB; 1.
DR InterPro; IPR014046; C-di-AMP_synthase.
DR InterPro; IPR034693; CdaS.
DR InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR InterPro; IPR019457; Uncharacterised_YojJ_N.
DR Pfam; PF02457; DAC; 1.
DR Pfam; PF10372; YojJ; 1.
DR PIRSF; PIRSF004793; UCP004793; 1.
DR SUPFAM; SSF143597; SSF143597; 1.
DR PROSITE; PS51794; DAC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Nucleotidyltransferase; Sporulation;
KW Transferase.
FT CHAIN 1..201
FT /note="Diadenylate cyclase CdaS"
FT /id="PRO_0000436101"
FT DOMAIN 54..201
FT /note="DAC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00838"
FT MUTAGEN 4
FT /note="W->A,D: Decrease in c-di-AMP synthesis."
FT /evidence="ECO:0000269|PubMed:26441857"
FT MUTAGEN 4
FT /note="W->G: Slight decrease in c-di-AMP synthesis."
FT /evidence="ECO:0000269|PubMed:26441857"
FT MUTAGEN 4
FT /note="W->K: Nearly complete loss of c-di-AMP synthesis."
FT /evidence="ECO:0000269|PubMed:26441857"
FT MUTAGEN 131..132
FT /note="DG->AA: Loss of c-di-AMP synthesis."
FT /evidence="ECO:0000269|PubMed:26441857"
FT MUTAGEN 163..165
FT /note="RHR->AAA: Loss of c-di-AMP synthesis."
FT /evidence="ECO:0000269|PubMed:26441857"
SQ SEQUENCE 201 AA; 22207 MW; E488834DD0839A28 CRC64;
MHEWGLSEEL KIQTKQMIEI AEKELSIMRN AIDKEDECIL CKMEDIHHML ANVQTLAATY
YIQAYLSPYT ESSSFITTAI QHLSARKHGA LIVVERNETL EALIQTGTTL NAHLTAPLLE
SIFYPGNPLH DGAVLVKNNH IVSAANILPL TKSTEVDPEL GTRHRAAIGL SEKSDALILV
VSEETGRTSF ALNGILYTIS L
