ID L8EPQ0_STRR1 Unreviewed; 352 AA.
AC L8EPQ0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:QST82764.1};
GN ORFNames=SRIM_023710 {ECO:0000313|EMBL:QST82764.1};
OS Streptomyces rimosus subsp. rimosus (strain ATCC 10970 / DSM 40260 / JCM
OS 4667 / NRRL 2234).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1265868 {ECO:0000313|EMBL:QST82764.1, ECO:0000313|Proteomes:UP000011074};
RN [1] {ECO:0000313|EMBL:QST82764.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82764.1};
RA Pethick F.E., MacFadyen A.C., Tang Z., Sangal V., Tze-Tze L., Chu J.,
RA Guo M., Kirby R., Hoskisson P.A., Herron P.R., Hunter I.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QST82764.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82764.1};
RA Algora L., Schniete J.K., MacFadyen A., Hoskisson P.A., Hunter I.S.,
RA Herron P.R.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QST82764.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82764.1};
RA Algora-Gallardo L., Schniete J.K., Mark D.R., Hunter I.S., Herron P.R.;
RT "Bilateral symmetry of linear streptomycete chromosomes.";
RL bioRxiv 0:0-0(2021).
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}.
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DR EMBL; CP048261; QST82764.1; -; Genomic_DNA.
DR AlphaFoldDB; L8EPQ0; -.
DR Proteomes; UP000011074; Chromosome.
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01438}.
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
FT BINDING 96..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01438"
SQ SEQUENCE 352 AA; 38082 MW; 575852E045796827 CRC64;
MRASLSAVAP GTALRDGLER ILRGNTGGLI VLGFDKTVES MCTGGFVLDV EFSATRLREL
CKLDGALVLD KDITKILRAG VQLVPDASIP TEETGTRHRT AQRVSIQAGF PVVSVSQSMR
LIALYVDGER RVLEESAAIL SRANQALATL ERYKLRLDEV AGTLSALEIE DLVTVRDVTA
VAQRLEMVRR IATEIAEYVV ELGTDGRLLS LQLDELIAGV EPERELVARD YVPEPTAKRS
RTVPEALSEL DALSHAELLE LPIVARALGY SGSPETLDSA VSPRGFRLLA KVPRLPGAVI
DRLVDHFGGL QKLLAASVDD LQAVDGVGEA RARSVREGLS RLAESSILER YV
//
