ID   DISA_CLOBB              Reviewed;         354 AA.
AC   B2TIF1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=DNA integrity scanning protein DisA {ECO:0000255|HAMAP-Rule:MF_01438};
DE   AltName: Full=Cyclic di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01438};
DE            Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01438};
DE   AltName: Full=Diadenylate cyclase {ECO:0000255|HAMAP-Rule:MF_01438};
DE            EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_01438};
GN   Name=disA {ECO:0000255|HAMAP-Rule:MF_01438}; OrderedLocusNames=CLL_A0213;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in a DNA-damage check-point that is active prior
CC       to asymmetric division when DNA is damaged. DisA forms globular foci
CC       that rapidly scan along the chromosomes during sporulation, searching
CC       for lesions. When a lesion is present, DisA pauses at the lesion site.
CC       This triggers a cellular response that culminates in a temporary block
CC       in sporulation initiation. {ECO:0000255|HAMAP-Rule:MF_01438}.
CC   -!- FUNCTION: Has also diadenylate cyclase activity, catalyzing the
CC       condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP
CC       acts as a signaling molecule that couples DNA integrity with
CC       progression of sporulation. The rise in c-di-AMP level generated by
CC       DisA while scanning the chromosome, operates as a positive signal that
CC       advances sporulation; upon encountering a lesion, the DisA focus
CC       arrests at the damaged site and halts c-di-AMP synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01438}.
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_01438};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01438};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000255|HAMAP-Rule:MF_01438}.
CC   -!- SIMILARITY: Belongs to the DisA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01438}.
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DR   EMBL; CP001056; ACD22782.1; -; Genomic_DNA.
DR   RefSeq; WP_012423627.1; NC_018648.1.
DR   AlphaFoldDB; B2TIF1; -.
DR   SMR; B2TIF1; -.
DR   EnsemblBacteria; ACD22782; ACD22782; CLL_A0213.
DR   KEGG; cbk:CLL_A0213; -.
DR   PATRIC; fig|935198.13.peg.187; -.
DR   HOGENOM; CLU_787128_0_0_9; -.
DR   OMA; VVRDYVP; -.
DR   OrthoDB; 1139866at2; -.
DR   Proteomes; UP000001195; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106408; F:diadenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0019932; P:second-messenger-mediated signaling; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.1260.110; -; 1.
DR   Gene3D; 3.40.1700.10; -; 1.
DR   HAMAP; MF_01438; DisA; 1.
DR   InterPro; IPR038331; DisA_sf.
DR   InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR   InterPro; IPR018906; DNA_integrity_scan_DisA_link.
DR   InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR   InterPro; IPR023763; DNA_integrity_scanning_protein.
DR   InterPro; IPR010994; RuvA_2-like.
DR   Pfam; PF02457; DAC; 1.
DR   Pfam; PF10635; DisA-linker; 1.
DR   SUPFAM; SSF143597; SSF143597; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   PROSITE; PS51794; DAC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Magnesium;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..354
FT                   /note="DNA integrity scanning protein DisA"
FT                   /id="PRO_1000145859"
FT   DOMAIN          6..144
FT                   /note="DAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01130"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT   BINDING         104..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
SQ   SEQUENCE   354 AA;  39844 MW;  AB6144306AF27971 CRC64;
     MRLEKGMKIK DTLKIMCPGT QLREGLENIL RAKTGGLIVI GDNKEVMDTV DGGFNLNSDY
     SPSYVYELAK MDGAIVISED LKKIVCANAQ LIPDPSIVTH ETGTRHRTAH RIAKQTNNIV
     IAISQRRNII TVYKGDIKYV LRDSSVILAR ANQAIQTLEK YVSVLERVIN NLNLLEFQDL
     TTLFDVVTAI QRTEMVMRIV EEINMYILEL GNEGRLISMQ LNELVKHIER DGILLIRDYC
     KDEDGHNEVY EQIQKLSATE LLDLDAIARV LGHAGESLVD TLISAKGYRI LGKVPRIPST
     VIENLIKEFK ELNSVIEADI DELDIVEGIG EARAKAIKDG LKRIREQILL NKKI