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DISA_BACAN
ID   DISA_BACAN              Reviewed;         357 AA.
AC   Q81VV7; Q6I4W1; Q6KYK5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 126.
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};
GN   OrderedLocusNames=BA_0082, GBAA_0082, BAS0083;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
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; AE016879; AAP24137.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT52420.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT29162.1; -; Genomic_DNA.
DR   RefSeq; NP_842651.1; NC_003997.3.
DR   RefSeq; WP_000392168.1; NZ_WXXJ01000051.1.
DR   RefSeq; YP_026369.1; NC_005945.1.
DR   AlphaFoldDB; Q81VV7; -.
DR   SMR; Q81VV7; -.
DR   IntAct; Q81VV7; 12.
DR   STRING; 261594.GBAA_0082; -.
DR   DNASU; 1085924; -.
DR   EnsemblBacteria; AAP24137; AAP24137; BA_0082.
DR   EnsemblBacteria; AAT29162; AAT29162; GBAA_0082.
DR   GeneID; 45020128; -.
DR   GeneID; 59159737; -.
DR   KEGG; ban:BA_0082; -.
DR   KEGG; bar:GBAA_0082; -.
DR   KEGG; bat:BAS0083; -.
DR   PATRIC; fig|198094.11.peg.80; -.
DR   eggNOG; COG1623; Bacteria.
DR   HOGENOM; CLU_787128_0_0_9; -.
DR   OMA; VVRDYVP; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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..357
FT                   /note="DNA integrity scanning protein DisA"
FT                   /id="PRO_0000255631"
FT   DOMAIN          8..146
FT                   /note="DAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01130"
FT   BINDING         75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT   BINDING         106..110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
SQ   SEQUENCE   357 AA;  40095 MW;  528BD57E5EBDF9E8 CRC64;
     MEENKQRVKS MINILQLVAP GTPLREGIDN VLRAQTGGLI VLGYNEQIKS IVDGGFHINC
     AFSPASLYEL AKMDGALILN ETGSKILIAN AQLVPESSID SIETGMRHRT AERVAKQTGS
     LVVAISQRRN VITLYQGNLR YTLKDIGVIL TKANQAIQTL EKYKAVWNDG ITNLGILEFE
     EVVTMSEVVH VLHSVEMVLR IKNEILSYIH ELGTEGRLIR LQLTELLADL EAEAALLIKD
     YYQEKTQDHH QILKKLQELA NTQLLEDSDL VKLLGYPGQT SLEESVTPRG YRITSKISRV
     PPLIIENLIN RFKTLQGVCR ATINELDDVE GIGEVRAKKI REGLKRIQEH LYMSRHN
 
 
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