DISA_BACAH
ID DISA_BACAH Reviewed; 357 AA.
AC A0R8F5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=BALH_0083;
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam;
RX PubMed=17337577; DOI=10.1128/jb.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
RN [2]
RP INTERACTION WITH RADA.
RX PubMed=23760274; DOI=10.1074/jbc.m113.464883;
RA Zhang L., He Z.G.;
RT "Radiation-sensitive gene A (RadA) targets DisA, DNA integrity scanning
RT protein A, to negatively affect cyclic di-AMP synthesis activity in
RT Mycobacterium smegmatis.";
RL J. Biol. Chem. 288:22426-22436(2013).
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 -!- ACTIVITY REGULATION: Diadenylate cyclase activity is inhibited by the
CC interaction with RadA. {ECO:0000250}.
CC -!- SUBUNIT: Homooctamer (By similarity). Interacts with RadA.
CC {ECO:0000255|HAMAP-Rule:MF_01438, ECO:0000269|PubMed:23760274}.
CC -!- SIMILARITY: Belongs to the DisA family. {ECO:0000255|HAMAP-
CC Rule:MF_01438}.
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DR EMBL; CP000485; ABK83498.1; -; Genomic_DNA.
DR RefSeq; WP_000392168.1; NC_008600.1.
DR AlphaFoldDB; A0R8F5; -.
DR SMR; A0R8F5; -.
DR EnsemblBacteria; ABK83498; ABK83498; BALH_0083.
DR GeneID; 45020128; -.
DR GeneID; 59159737; -.
DR KEGG; btl:BALH_0083; -.
DR HOGENOM; CLU_787128_0_0_9; -.
DR OMA; VVRDYVP; -.
DR Proteomes; UP000000761; 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 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Magnesium;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..357
FT /note="DNA integrity scanning protein DisA"
FT /id="PRO_1000017366"
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
