ID A0A0S9DB23_9MICC Unreviewed; 358 AA.
AC A0A0S9DB23;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=ASF21_01615 {ECO:0000313|EMBL:KQO03061.1};
OS Arthrobacter sp. Leaf234.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQO03061.1, ECO:0000313|Proteomes:UP000053418};
RN [1] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 likely acts as a signaling molecule that may couple DNA integrity with
CC a cellular process. {ECO:0000256|HAMAP-Rule:MF_01438}.
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: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:KQO03061.1}.
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DR EMBL; LMLU01000001; KQO03061.1; -; Genomic_DNA.
DR RefSeq; WP_055765885.1; NZ_LMLU01000001.1.
DR AlphaFoldDB; A0A0S9DB23; -.
DR STRING; 1736303.ASF21_01615; -.
DR Proteomes; UP000053418; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01438}.
FT DOMAIN 6..145
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
FT COILED 151..178
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT BINDING 104..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
SQ SEQUENCE 358 AA; 38996 MW; B2AA6AA785DA6158 CRC64;
MVRSPEDSLK ATLARVAPGT HLRDGLERIL RGRTGALIVL GFDRTVDSIC SGGFDIGIEF
SPTRLRELAK MDGAIVCDKD ASRILRAAVQ LVPDHTIETQ ESGTRHRTAE RVAKQTGLPV
ISVSQSMQII ALYIDGLRHV LEGSEPVLAR ANQALATLER YRARLDQVTN SLSALEIEAM
VTVRDVAVTL QRQEMVRRIS EEISQYVLEL GVDGRLLSLQ VEELTTGLGP GSEMVLRDYM
DLGNSTAPLD ERVATLQGFS STDLIDLGTI ASVLGFNPSV DSLEAVIQPK GYRLLSGIKA
VPPAVANRLV DHFDGLQNLM AANIEDLMAV DGIGEQRART VREGLSRIAE TSLLDRFM
//
