ID A0A0B0D7E1_9BACI Unreviewed; 357 AA.
AC A0A0B0D7E1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=DNA integrity scanning protein DisA {ECO:0000256|HAMAP-Rule:MF_01438};
DE AltName: Full=Cyclic di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_01438};
DE Short=c-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_01438};
DE AltName: Full=Diadenylate cyclase {ECO:0000256|HAMAP-Rule:MF_01438};
DE EC=2.7.7.85 {ECO:0000256|HAMAP-Rule:MF_01438};
GN Name=disA {ECO:0000256|HAMAP-Rule:MF_01438};
GN ORFNames=LD39_10950 {ECO:0000313|EMBL:KHE70872.1};
OS Halobacillus sp. BBL2006.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE70872.1, ECO:0000313|Proteomes:UP000030879};
RN [1] {ECO:0000313|EMBL:KHE70872.1, ECO:0000313|Proteomes:UP000030879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBL2006 {ECO:0000313|EMBL:KHE70872.1,
RC ECO:0000313|Proteomes:UP000030879};
RA Kirchner G., Treves D., Francis J.III.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BBL2006.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01438}.
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:0000256|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:0000256|ARBA:ARBA00000877, ECO:0000256|HAMAP-
CC Rule:MF_01438};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01438};
CC -!- SUBUNIT: Homooctamer. {ECO:0000256|HAMAP-Rule:MF_01438}.
CC -!- SIMILARITY: Belongs to the DisA family. {ECO:0000256|HAMAP-
CC Rule:MF_01438}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHE70872.1}.
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DR EMBL; JRNX01000347; KHE70872.1; -; Genomic_DNA.
DR RefSeq; WP_035546234.1; NZ_JRNX01000347.1.
DR AlphaFoldDB; A0A0B0D7E1; -.
DR OrthoDB; 41841at2; -.
DR Proteomes; UP000030879; Unassembled WGS sequence.
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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 1.20.1260.110; DNA integrity scanning linker region; 1.
DR Gene3D; 3.40.1700.10; DNA integrity scanning protein, DisA, N-terminal domain; 1.
DR HAMAP; MF_01438; DisA; 1.
DR InterPro; IPR041663; DisA/LigA_HHH.
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 PANTHER; PTHR34185; DIADENYLATE CYCLASE; 1.
DR PANTHER; PTHR34185:SF3; DNA INTEGRITY SCANNING PROTEIN DISA; 1.
DR Pfam; PF02457; DAC; 1.
DR Pfam; PF10635; DisA-linker; 1.
DR Pfam; PF12826; HHH_2; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR SUPFAM; SSF143597; YojJ-like; 1.
DR PROSITE; PS51794; DAC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01438};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01438};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01438};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01438};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01438};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01438};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01438}; Reference proteome {ECO:0000313|Proteomes:UP000030879};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01438}.
FT DOMAIN 8..146
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT BINDING 106..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
SQ SEQUENCE 357 AA; 40424 MW; 702E915E0B74041F CRC64;
MEWHEMKDNG IGEILKLVAP GTPLRDGIDN VLRANTGGLI VLGYGDDIRD LVDGGFHIQA
DFTPAHLYEL AKMDGALILN DEGSKILFAN AQLMPDPHIY STETGMRHRT AERVAKQTGS
LVIAISQRRN VITLYKGSLR YSLKDIGVIL TKANQAIQTL EKYKNVLDQS ITNLGAMEFE
NMVSFSEVVQ VVHRVEMVLR TKTEIINYVN ELGTEGRLIQ LQMTELVSNI EEEAALLLKD
YSKRPDYEPY YILRKMQEVT NTELLSDEQI LKLLGYSPNT KMADPIHPRG YRILSRIPRL
PPLIIEHLVE RFGTLDDMIQ ASTKELVEVD GVGEIRASKI RDGLERIQEQ LFVDRHI
//