ID A0A368YHF0_9FIRM Unreviewed; 360 AA.
AC A0A368YHF0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=DER71_1367 {ECO:0000313|EMBL:RCW79660.1};
OS Halanaerobium sp. DL-01.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=1653064 {ECO:0000313|EMBL:RCW79660.1, ECO:0000313|Proteomes:UP000253016};
RN [1] {ECO:0000313|EMBL:RCW79660.1, ECO:0000313|Proteomes:UP000253016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-01 {ECO:0000313|EMBL:RCW79660.1,
RC ECO:0000313|Proteomes:UP000253016};
RA Wrighton K.;
RT "Subsurface microbial communities from deep shales in Ohio and West
RT Virginia, USA.";
RL Submitted (JUL-2018) 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:RCW79660.1}.
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DR EMBL; QPJN01000036; RCW79660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368YHF0; -.
DR OrthoDB; 41841at2; -.
DR Proteomes; UP000253016; 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; 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; IPR000445; HhH_motif.
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; PF00633; HHH; 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:UP000253016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01438}.
FT DOMAIN 5..143
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
SQ SEQUENCE 360 AA; 40548 MW; 47333E689DB4FE81 CRC64;
MEQYDEKLLD ILKILAPGTD FREGLENILR AQTGALLIVG DSEETLSLVN DGFEINTSFT
PTKLYELAKM DGAIVLDRDA EKILVANAQL IPDPTIPSTE TGTRHKTAER VAKQTGELVI
AISERRSIIT IYKADYKHIL EDIGVILTKA NQAVQTLEKY RSVFDQALTN LSALEFEDLV
TISDVVTVIQ RTEMVLKIQR EIEKYISELG TEGRLIKMQL EELVTNVKEE GILLIKDYIA
EAKDDEEQPK PENLLEELTD WSSDEILTLN TISKALGYSG SVNALDQSIS PRGYRILRKI
PRLPMPVIEN LVEHFDKLQE VIRASVDELD DVDGIGEVRA QAIKDGLRRL RDQVLLDRHI
//
