(data stored in ACNUC7421 zone)

SWISSPROT: C8W3V6_DESAS

ID   C8W3V6_DESAS            Unreviewed;       359 AA.
AC   C8W3V6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 67.
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   OrderedLocusNames=Dtox_0257 {ECO:0000313|EMBL:ACV61210.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61210.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61210.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Has also diadenylate cyclase activity, catalyzing the
CC       condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-
CC       di-AMP acts as a signaling molecule that couples DNA integrity
CC       with progression of sporulation. The rise in c-di-AMP level
CC       generated by DisA while scanning the chromosome, operates as a
CC       positive signal that advances sporulation; upon encountering a
CC       lesion, the DisA focus arrests at the damaged site and halts c-di-
CC       AMP synthesis. {ECO:0000256|HAMAP-Rule:MF_01438}.
CC   -!- FUNCTION: Participates in a DNA-damage check-point that is active
CC       prior to asymmetric division when DNA is damaged. DisA forms
CC       globular foci that rapidly scan along the chromosomes during
CC       sporulation, searching for lesions. When a lesion is present, DisA
CC       pauses at the lesion site. This triggers a cellular response that
CC       culminates in a temporary block in sporulation initiation.
CC       {ECO:0000256|HAMAP-Rule:MF_01438}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP = c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500;
CC         EC=2.7.7.85; Evidence={ECO:0000256|HAMAP-Rule:MF_01438,
CC         ECO:0000256|SAAS:SAAS01115408};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01438, ECO:0000256|SAAS:SAAS00724644};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|HAMAP-Rule:MF_01438}.
CC   -!- SIMILARITY: Belongs to the DisA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01438, ECO:0000256|SAAS:SAAS00724629}.
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DR   EMBL; CP001720; ACV61210.1; -; Genomic_DNA.
DR   RefSeq; WP_015755931.1; NC_013216.1.
DR   STRING; 485916.Dtox_0257; -.
DR   EnsemblBacteria; ACV61210; ACV61210; Dtox_0257.
DR   KEGG; dae:Dtox_0257; -.
DR   eggNOG; ENOG4105E59; Bacteria.
DR   eggNOG; COG1623; LUCA.
DR   HOGENOM; HOG000236713; -.
DR   KO; K07067; -.
DR   OMA; SKMDGAI; -.
DR   OrthoDB; 1139866at2; -.
DR   BioCyc; DACE485916:G1GFV-267-MONOMER; -.
DR   Proteomes; UP000002217; 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; C8W3V6.
DR   SWISS-2DPAGE; C8W3V6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00772210};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00724631};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00724636};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00724650};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00724630};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00772222};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00772249};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01438,
KW   ECO:0000256|SAAS:SAAS00772224}.
FT   DOMAIN        7    145       DAC. {ECO:0000259|PROSITE:PS51794}.
FT   NP_BIND     105    109       ATP. {ECO:0000256|HAMAP-Rule:MF_01438}.
FT   BINDING      74     74       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01438}.
FT   BINDING      92     92       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01438}.
SQ   SEQUENCE   359 AA;  39913 MW;  E35B8EAB3AFC127C CRC64;
     MKEEKAEDQL LKVLRFVAPG TSLREGLENI LRAKTGGLVV VGDYPEVLDI AEGGFAINAD
     YSSANLYELA KMDGAIVLSE DAKRILAANV QLIPSQNIPS SETGIRHRTS ERVARQTNAL
     VIAISQRRSV ISVYKGNLKY VLRDLGVILT KANQAVQTLE KYRAVSDKVL VNLSILEYDG
     VVTLFDVAKV IQRVEMVLRI VKEIEKYISE LGTEGRLITM QLEELLANVA EEGFLVIQDY
     GTVLEEKPPQ SIMKIIGSWP AEDLLDLSLI ARALGYPGSS GILDQSVFPR GYRILEKLPR
     LPFPVIENLV QRFGTLSKVL VATIEELDEV EGIGEVRARS IKKGLSRYRE QLLTQERHT
//

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