DISA_BACCR
ID DISA_BACCR Reviewed; 357 AA.
AC Q81J64;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DNA integrity scanning protein DisA {ECO:0000255|HAMAP-Rule:MF_01438};
DE AltName: Full=Cyclic di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01438};
DE Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01438};
DE AltName: Full=Diadenylate cyclase {ECO:0000255|HAMAP-Rule:MF_01438};
DE EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_01438};
GN Name=disA {ECO:0000255|HAMAP-Rule:MF_01438}; OrderedLocusNames=BC_0104;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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:0000255|HAMAP-Rule:MF_01438}.
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:0000255|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:0000255|HAMAP-Rule:MF_01438};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01438};
CC -!- SUBUNIT: Homooctamer. {ECO:0000255|HAMAP-Rule:MF_01438}.
CC -!- SIMILARITY: Belongs to the DisA family. {ECO:0000255|HAMAP-
CC Rule:MF_01438}.
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DR EMBL; AE016877; AAP07186.1; -; Genomic_DNA.
DR RefSeq; NP_829985.1; NC_004722.1.
DR RefSeq; WP_000392163.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81J64; -.
DR SMR; Q81J64; -.
DR STRING; 226900.BC_0104; -.
DR EnsemblBacteria; AAP07186; AAP07186; BC_0104.
DR GeneID; 67504790; -.
DR KEGG; bce:BC0104; -.
DR PATRIC; fig|226900.8.peg.106; -.
DR HOGENOM; CLU_787128_0_0_9; -.
DR OMA; VVRDYVP; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
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; 1.20.1260.110; -; 1.
DR Gene3D; 3.40.1700.10; -; 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; IPR010994; RuvA_2-like.
DR Pfam; PF02457; DAC; 1.
DR Pfam; PF10635; DisA-linker; 1.
DR SUPFAM; SSF143597; SSF143597; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR PROSITE; PS51794; DAC; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Magnesium;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..357
FT /note="DNA integrity scanning protein DisA"
FT /id="PRO_0000255633"
FT DOMAIN 8..146
FT /note="DAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01130"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT BINDING 106..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
SQ SEQUENCE 357 AA; 40041 MW; 56CA5E0342CAE2EF CRC64;
MEENKQRVKS MINILQLVAP GTPLREGIDN VLRAQTGGLI VLGYNEQIKS IVDGGFHINC
AFSPASLYEL AKMDGALILN ETGSKILIAN AQLVPDSSID SIETGMRHRT AERVAKQTGS
LVVAISQRRN VITLYQGNLR YTLKDIGVIL TKANQAIQTL EKYKAVWNDG ITNLGILEFE
EVVTMSEVVH VLHSVEMVLR IKNEILSYIH ELGTEGRLIR LQLTELLADL EAEAALLIKD
YHQEKTQDHH QILKKLQDLA NTQLLEDSDL VKLLGYPGQT SLEESVTPRG YRITSKISRV
PPLIIENLIN RFKTLQGVCR ATINELDDVE GIGEVRAKKI REGLKRIQEH LYMSRHN
