ID A0A132NE57_9ACTN Unreviewed; 367 AA.
AC A0A132NE57;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=LI90_549 {ECO:0000313|EMBL:KWW98919.1}, TH66_18510
GN {ECO:0000313|EMBL:KWW97575.1}, TR74_15685
GN {ECO:0000313|EMBL:KWX08287.1};
OS Carbonactinospora thermoautotrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Carbonactinosporaceae; Carbonactinospora.
OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWX08287.1, ECO:0000313|Proteomes:UP000070598};
RN [1] {ECO:0000313|Proteomes:UP000070598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBT1 {ECO:0000313|Proteomes:UP000070598};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KWX08287.1, ECO:0000313|Proteomes:UP000070659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBT1 {ECO:0000313|EMBL:KWX08287.1,
RC ECO:0000313|Proteomes:UP000070659};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000070188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:KWW98919.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|EMBL:KWW98919.1};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Woodward J., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-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:KWX08287.1}.
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; JYIJ01000019; KWW97575.1; -; Genomic_DNA.
DR EMBL; LAXD01000001; KWW98919.1; -; Genomic_DNA.
DR EMBL; JYIK01000995; KWX08287.1; -; Genomic_DNA.
DR RefSeq; WP_066883870.1; NZ_LAXD01000001.1.
DR AlphaFoldDB; A0A132NE57; -.
DR STRING; 1469144.LI90_549; -.
DR PATRIC; fig|1469144.10.peg.647; -.
DR OrthoDB; 41841at2; -.
DR Proteomes; UP000070188; Unassembled WGS sequence.
DR Proteomes; UP000070598; Unassembled WGS sequence.
DR Proteomes; UP000070659; 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:UP000070188};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01438}.
FT DOMAIN 14..152
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT BINDING 112..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
SQ SEQUENCE 367 AA; 39996 MW; D8E94616E117C303 CRC64;
MATSDRADKG TNPDALLRAT LARVAPGTAL RDGLERILRG NTGALIVLGY DKTVEQLCTG
GFVLDVEFSS TRLRELCKMD GAVVLDRDCT RILRAGVHLV PDPSIPTEET GTRHRTAERV
AKQTGFPVIS VSQSMRLIAL YVAGRRYVLE DSGAILSRAN QALATLERYK LRLDEVSGTL
SALEIEDLVT VRDVAAVAQR LEMVRRIASE IEGYVVELGN DGRLLALQLD ELVAGVDADR
ELVARDYLPE RGGKRTRTVE DVLRDLDELS SNELLDLSLV AKALGYAGAD ALDAAVSPRG
YRLLAKVPRL PNLVIDRLVE HFGSLQKLLA ASIDDLQAVE GVGESRARTV REGLSRLAES
SILERYV
//
