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DISA_FUSNN
ID   DISA_FUSNN              Reviewed;         349 AA.
AC   Q8RGW9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=FN0158;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL94364.1; -; Genomic_DNA.
DR   RefSeq; NP_603065.1; NC_003454.1.
DR   AlphaFoldDB; Q8RGW9; -.
DR   SMR; Q8RGW9; -.
DR   STRING; 190304.FN0158; -.
DR   EnsemblBacteria; AAL94364; AAL94364; FN0158.
DR   KEGG; fnu:FN0158; -.
DR   PATRIC; fig|190304.8.peg.738; -.
DR   eggNOG; COG1623; Bacteria.
DR   HOGENOM; CLU_787128_0_0_0; -.
DR   InParanoid; Q8RGW9; -.
DR   OMA; VVRDYVP; -.
DR   BioCyc; FNUC190304:G1FZS-761-MON; -.
DR   Proteomes; UP000002521; Chromosome.
DR   GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
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   Pfam; PF02457; DAC; 1.
DR   Pfam; PF10635; DisA-linker; 1.
DR   SUPFAM; SSF143597; SSF143597; 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..349
FT                   /note="DNA integrity scanning protein DisA"
FT                   /id="PRO_0000255646"
FT   DOMAIN          3..143
FT                   /note="DAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01130"
FT   BINDING         70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT   BINDING         88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT   BINDING         101..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
SQ   SEQUENCE   349 AA;  39960 MW;  D14E48EC36B83824 CRC64;
     MTKQDLMDII VKVAPGSPLR EGVDYILDAG IGALIIIGYD DEVEKVRDGG FLIDCDYTPE
     RIFELSKMDG AIILNDDCSK ILYANVHVQP DNSYSTTESG TRHRTAERAA KHLKREVVAI
     SERKKNVTLY KGNLKYRLKN FDELNIEVGQ VLKTLESYRH VLNRSLDSLT ILELDDLVTV
     LDVANTLQRF EMVRRISEEI TRYLLELGSR GRLVNMQVSE LIWDLDEEEE SFLKDYIDDE
     TDTDSVRRYL HSLSDSELLE VENVVVALGY SKSSSVFDNK IAAKGYRVLE KISKLTKKDV
     EKIVNTYKDI SEIQEVTDED FSAIKISKFK IKALRAGINR LKFTIEMQR
 
 
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