(data stored in ACNUC9435 zone)

SWISSPROT: DISA_CLOD6

ID   DISA_CLOD6              Reviewed;         356 AA.
AC   Q18CB2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   11-DEC-2019, entry version 81.
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=CD630_00280;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
RN   [2]
RP   FUNCTION.
RX   PubMed=25965978; DOI=10.1021/jacs.5b00275;
RA   Kellenberger C.A., Chen C., Whiteley A.T., Portnoy D.A., Hammond M.C.;
RT   "RNA-based fluorescent biosensors for live cell imaging of second messenger
RT   cyclic di-AMP.";
RL   J. Am. Chem. Soc. 137:6432-6435(2015).
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)
CC       (PubMed:25965978). c-di-AMP acts as a signaling molecule that couples
CC       DNA integrity with progression of sporulation. The rise in c-di-AMP
CC       level generated by DisA while scanning the chromosome, operates as a
CC       positive signal that advances sporulation; upon encountering a lesion,
CC       the DisA focus arrests at the damaged site and halts c-di-AMP
CC       synthesis. {ECO:0000255|HAMAP-Rule:MF_01438,
CC       ECO:0000269|PubMed:25965978}.
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}.
DR   EMBL; AM180355; CAJ66842.1; -; Genomic_DNA.
DR   RefSeq; WP_004453975.1; NZ_CP010905.2.
DR   RefSeq; YP_001086491.1; NC_009089.1.
DR   SMR; Q18CB2; -.
DR   STRING; 272563.CD630_00280; -.
DR   PRIDE; Q18CB2; -.
DR   EnsemblBacteria; CAJ66842; CAJ66842; CD630_00280.
DR   GeneID; 4916497; -.
DR   KEGG; cdf:CD630_00280; -.
DR   KEGG; pdc:CDIF630_00090; -.
DR   PATRIC; fig|272563.120.peg.32; -.
DR   eggNOG; ENOG4105E59; Bacteria.
DR   eggNOG; COG1623; LUCA.
DR   HOGENOM; HOG000236713; -.
DR   KO; K07067; -.
DR   OMA; SKMDGAI; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; 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; PF10635; DisA-linker; 1.
DR   Pfam; PF02457; DisA_N; 1.
DR   SUPFAM; SSF143597; SSF143597; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   PROSITE; PS51794; DAC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q18CB2.
DR   SWISS-2DPAGE; Q18CB2.
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Magnesium;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..356
FT                   /note="DNA integrity scanning protein DisA"
FT                   /id="PRO_1000017367"
FT   DOMAIN          7..147
FT                   /note="DAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01130"
FT   NP_BIND         105..109
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT   BINDING         74
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
FT   BINDING         92
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01438"
SQ   SEQUENCE   356 AA;  40369 MW;  F2DBAF4E4DE386AA CRC64;
     MENFLDNKNM LYALKMISPG TPLRLGLNNV LRAKTGGLIV IATNEDVMKI VDGGFAINAE
     YSPSYLYELA KMDGAIVLSG DVKKILFANA QLIPDYFIET SETGTRHRTA ERVAKQTGAI
     VIGISQRRNV ITVYRGNEKY VVEDISKIFT KANQAIQTLE KYKTVLDQAV TNLNALEFND
     LVTIYDVALV MQKMEMVMRV TSIIEKYVIE LGDEGTLVSM QLEELMGTTR IDQKLIFKDY
     NKENTEIKEL MKKVKNLNSE ELIELVNMAK LLGYSGFSES MDMPIKTRGY RILSKIHRLP
     TAIIENLVNY FENFQQILDA SIEELDEVEG IGEIRATYIK NGLIKMKQLV LLDRHI
//

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