ID L8TRR7_9MICC Unreviewed; 358 AA.
AC L8TRR7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
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 ECO:0000313|EMBL:TDL36756.1};
GN ORFNames=E2R57_12485 {ECO:0000313|EMBL:TDL36756.1}, G205_11127
GN {ECO:0000313|EMBL:ELT44540.1};
OS Arthrobacter nitrophenolicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT44540.1, ECO:0000313|Proteomes:UP000011189};
RN [1] {ECO:0000313|EMBL:ELT44540.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJCon {ECO:0000313|EMBL:ELT44540.1};
RA Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.S.;
RT "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT Arthrobacter sp. Strain SJCon.";
RL Genome Announc. 1:E00058-13(2013).
RN [2] {ECO:0000313|Proteomes:UP000011189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJCon {ECO:0000313|Proteomes:UP000011189};
RX PubMed=23516196; DOI=10.1128/genomeA.00058-13;
RA Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.;
RT "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT Arthrobacter sp. Strain SJCon.";
RL Genome Announc. 1:e0005813-e0005813(2013).
RN [3] {ECO:0000313|EMBL:TDL36756.1, ECO:0000313|Proteomes:UP000294621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-A1 {ECO:0000313|EMBL:TDL36756.1,
RC ECO:0000313|Proteomes:UP000294621};
RA Steinbock B., Bechtold R., Sevigny J.L., Thomas D., Cuthill L.R.,
RA Aveiro Johannsen E.J., Thomas K., Ghosh A.;
RT "Genome Sequencing and Assembly of Various Microbes Isolated from Partially
RT Reclaimed Soil and Acid Mine Drainage (AMD) Site.";
RL Submitted (MAR-2019) 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:ELT44540.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOFD01000021; ELT44540.1; -; Genomic_DNA.
DR EMBL; SMZQ01000006; TDL36756.1; -; Genomic_DNA.
DR RefSeq; WP_009357808.1; NZ_SMZQ01000006.1.
DR AlphaFoldDB; L8TRR7; -.
DR STRING; 683150.G205_11127; -.
DR PATRIC; fig|683150.5.peg.2197; -.
DR OrthoDB; 41841at2; -.
DR Proteomes; UP000011189; Unassembled WGS sequence.
DR Proteomes; UP000294621; 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:UP000011189};
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 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; 38580 MW; E8AD8A3340B14566 CRC64;
MARSPEESLR ATLGRVAPGT PLRDGLERIL RGRTGALIVL GSDRTVDSIC SGGFDIGIEF
SPTRLRELAK MDGAIICDRD AGNILRAAVQ LVPDSSIETQ ESGTRHRTAE RVAIQTGVPV
ISVSQSMQII ALYVNGLRHV LEGSEKVLAR ANQALATLER YRSRLDQVTS SLSALEIEAM
VTVRDVAVTL QRQEMVRRIS EEISQYVLEL GEDGRLLSLQ LDELTVGRGP GSDVIIRDYA
SPDASPEDIE KAVSALVNLG PTELIDLGKI SGIVGFAGGE ANLDAVVQPR GYRLLSGLKA
VPKAVADRLV DHFGGLQFLM AATIDDLMTV DGIGDQRART VREGLSRMAE ASLLDRFL
//
