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DISA_COREF
ID   DISA_COREF              Reviewed;         356 AA.
AC   Q8FMH9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=CE2525;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
CC   -!- FUNCTION: Participates in a DNA-damage check-point. DisA forms globular
CC       foci that rapidly scan along the chromosomes searching for lesions.
CC       {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       likely acts as a signaling molecule that may couple DNA integrity with
CC       a cellular process. {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; BA000035; BAC19335.1; -; Genomic_DNA.
DR   RefSeq; WP_006769113.1; NZ_GG700685.1.
DR   AlphaFoldDB; Q8FMH9; -.
DR   SMR; Q8FMH9; -.
DR   STRING; 196164.23494368; -.
DR   EnsemblBacteria; BAC19335; BAC19335; BAC19335.
DR   KEGG; cef:CE2525; -.
DR   eggNOG; COG1623; Bacteria.
DR   HOGENOM; CLU_787128_0_0_11; -.
DR   OMA; VVRDYVP; -.
DR   OrthoDB; 1139866at2; -.
DR   Proteomes; UP000001409; 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..356
FT                   /note="DNA integrity scanning protein DisA"
FT                   /id="PRO_0000255643"
FT   DOMAIN          11..149
FT                   /note="DAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01130"
FT   BINDING         78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT   BINDING         109..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
SQ   SEQUENCE   356 AA;  39368 MW;  0749DAB5CBCBC643 CRC64;
     MSTTTDILPD VHTMRDTLQR LAPGTPLRDG LDRIVRGHTG ALIVLGDEEN VTSICDGGFE
     FDVTFAATRL RELCKMDGAV VLSSDGERIK RANVQLIPSP SWPTQESGTR HRSAERTALQ
     TGVPVIAVSE SQNTITLYVE GKSHILEEPS TLLNRANQAL GTMERYRDRL DQVNTRLHMA
     ELHNYATVID VVSVIQREEM LRRVGETIDT NVLELGREAK QIQIQLTELR GDNDRERGYI
     IADYLVTDGI PTDETITEAL EAVSGLDDKS LMKPSNIARI LGLPPTEEAL DEPVVPRGYR
     TLNRVPRVQK FLMDKLVGEF GNLHALTSAS VEEISAVDGV GSLWARHITD GLARLT
 
 
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