ID   DISA_CLOPE              Reviewed;         354 AA.
AC   Q8XHQ0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=CPE2432;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000016; BAB82138.1; -; Genomic_DNA.
DR   RefSeq; WP_003452233.1; NC_003366.1.
DR   AlphaFoldDB; Q8XHQ0; -.
DR   SMR; Q8XHQ0; -.
DR   STRING; 195102.gene:10491750; -.
DR   EnsemblBacteria; BAB82138; BAB82138; BAB82138.
DR   KEGG; cpe:CPE2432; -.
DR   HOGENOM; CLU_787128_0_0_9; -.
DR   OMA; VVRDYVP; -.
DR   Proteomes; UP000000818; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..354
FT                   /note="DNA integrity scanning protein DisA"
FT                   /id="PRO_0000255641"
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;  40004 MW;  82ED4B12098E50D3 CRC64;
     MRTVHDDELK KILKIMSPGT SLREGLDNIL RAKTGGLIVL GDNEEILDLV DGGFNINSEY
     SPAYIYELAK MDGALVLTSD RKRILYANAQ LMPNQSISTF ETGTRHRTAQ RVAKQTNKIA
     IAISQRRNII TVYKGDIKYV LRDSAVILSK ANQAIQTLEK YVAVLERVTN NLNILEFQDL
     ATLFDVTTAI QRTEMVMRIV EEIEGYIIEL GNEGRLISMQ LNELVRSIEQ DGVLLIRDYC
     YDKMEYNDVY KEIQELSAED LLDLDIIAKE LGYVGKSLID TLVSPRGYRI SNKVPRIPSN
     VIENLVGHFG KLKYILEAGN EELDQVEGIG EARARAIKNG LRRIREQVAL NKNL