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DNA integrity scanning protein DisA (Cyclic di-AMP synthase) (c-di-AMP synthase) (Diadenylate cyclase) (EC 2.7.7.85)

 DISA_THEMA              Reviewed;         357 AA.
Q9WY43;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
28-MAR-2018, entry version 108.
RecName: Full=DNA integrity scanning protein DisA {ECO:0000255|HAMAP-Rule:MF_01438};
AltName: Full=Cyclic di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01438};
Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01438};
AltName: Full=Diadenylate cyclase {ECO:0000255|HAMAP-Rule:MF_01438};
EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_01438, ECO:0000269|PubMed:18439896};
Name=disA {ECO:0000255|HAMAP-Rule:MF_01438};
OrderedLocusNames=TM_0200;
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
NCBI_TaxID=243274;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
PubMed=10360571; DOI=10.1038/20601;
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
"Evidence for lateral gene transfer between Archaea and Bacteria from
genome sequence of Thermotoga maritima.";
Nature 399:323-329(1999).
[2]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF APOPROTEIN AND IN COMPLEXES
WITH ATP ANALOGS OR PRODUCT C-DI-AMP, FUNCTION, CATALYTIC ACTIVITY,
SUBSTRATE SPECIFICITY, SUBUNIT, AND DOMAIN.
PubMed=18439896; DOI=10.1016/j.molcel.2008.02.020;
Witte G., Hartung S., Buttner K., Hopfner K.P.;
"Structural biochemistry of a bacterial checkpoint protein reveals
diadenylate cyclase activity regulated by DNA recombination
intermediates.";
Mol. Cell 30:167-178(2008).
[3]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH PRODUCT
C-DI-AMP OR ATP ANALOGS AND METAL, FUNCTION, COFACTOR, ENZYME
REGULATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASP-75;
107-THR--THR-111; 108-ARG--ARG-110; 128-ARG--ARG-130 AND ARG-130.
PubMed=26014055; DOI=10.1042/BJ20150373;
Muller M., Deimling T., Hopfner K.P., Witte G.;
"Structural analysis of the diadenylate cyclase reaction of DNA-
integrity scanning protein A (DisA) and its inhibition by 3'-dATP.";
Biochem. J. 469:367-374(2015).
-!- FUNCTION: Participates in a DNA-damage check-point. DisA forms
globular foci that rapidly scan along the chromosomes searching
for lesions. {ECO:0000255|HAMAP-Rule:MF_01438}.
-!- FUNCTION: Has diadenylate cyclase activity, catalyzing the
condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP)
(PubMed:18439896, PubMed:26014055). c-di-AMP likely acts as a
signaling molecule that may couple DNA integrity with a cellular
process. This rate-limiting step is the accessibility of the
active site; mutating the possible exit tunnel (residues 128-130)
increases product 2-fold despite Arg-130 being important for ATP-
binding (PubMed:26014055). Does not convert GTP to c-di-GMP
(PubMed:18439896). {ECO:0000255|HAMAP-Rule:MF_01438,
ECO:0000269|PubMed:18439896, ECO:0000269|PubMed:26014055}.
-!- CATALYTIC ACTIVITY: 2 ATP = 2 diphosphate + cyclic di-3',5'-
adenylate. {ECO:0000255|HAMAP-Rule:MF_01438,
ECO:0000269|PubMed:18439896}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01438,
ECO:0000305|PubMed:26014055};
Note=Crystallized with Mn(2+) to trap in the pre-reaction state.
{ECO:0000269|PubMed:26014055};
-!- ENZYME REGULATION: Inhibited by 3'-dATP.
{ECO:0000269|PubMed:26014055}.
-!- SUBUNIT: Homooctamer. {ECO:0000255|HAMAP-Rule:MF_01438,
ECO:0000269|PubMed:18439896, ECO:0000269|PubMed:26014055}.
-!- DOMAIN: Consists of three domains: an N-terminal globular domain
with diadenylate-cyclase (DAC) activity, a central helical domain
and a C-terminal DNA-binding domain. {ECO:0000269|PubMed:18439896,
ECO:0000269|PubMed:26014055}.
-!- SIMILARITY: Belongs to the DisA family. {ECO:0000255|HAMAP-
Rule:MF_01438}.
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EMBL; AE000512; AAD35292.1; -; Genomic_DNA.
PIR; B72405; B72405.
RefSeq; NP_228015.1; NC_000853.1.
RefSeq; WP_010865072.1; NZ_CP011107.1.
PDB; 3C1Y; X-ray; 2.10 A; A/B=1-357.
PDB; 3C1Z; X-ray; 2.30 A; A/B=1-357.
PDB; 3C21; X-ray; 2.70 A; A/B=1-357.
PDB; 3C23; X-ray; 2.50 A; A/B=1-357.
PDB; 4YVZ; X-ray; 2.50 A; A/B=1-357.
PDB; 4YXJ; X-ray; 2.55 A; A/B=1-357.
PDB; 4YXM; X-ray; 2.25 A; A/B=1-357.
PDBsum; 3C1Y; -.
PDBsum; 3C1Z; -.
PDBsum; 3C21; -.
PDBsum; 3C23; -.
PDBsum; 4YVZ; -.
PDBsum; 4YXJ; -.
PDBsum; 4YXM; -.
ProteinModelPortal; Q9WY43; -.
SMR; Q9WY43; -.
STRING; 243274.TM0200; -.
EnsemblBacteria; AAD35292; AAD35292; TM_0200.
GeneID; 897070; -.
KEGG; tma:TM0200; -.
PATRIC; fig|243274.5.peg.202; -.
eggNOG; ENOG4105E59; Bacteria.
eggNOG; COG1623; LUCA.
InParanoid; Q9WY43; -.
KO; K07067; -.
OMA; SKMDGAI; -.
BioCyc; TMAR243274:G1H0Q-749-MONOMER; -.
BRENDA; 2.7.7.85; 6331.
EvolutionaryTrace; Q9WY43; -.
Proteomes; UP000008183; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
Gene3D; 1.20.1260.110; -; 1.
Gene3D; 3.40.1700.10; -; 1.
HAMAP; MF_01438; DisA; 1.
InterPro; IPR038331; DisA_sf.
InterPro; IPR036888; DNA_integrity_DisA_N_sf.
InterPro; IPR018906; DNA_integrity_scan_DisA_link.
InterPro; IPR003390; DNA_integrity_scan_DisA_N.
InterPro; IPR023763; DNA_integrity_scanning_protein.
InterPro; IPR000445; HhH_motif.
InterPro; IPR010994; RuvA_2-like.
Pfam; PF10635; DisA-linker; 1.
Pfam; PF02457; DisA_N; 1.
Pfam; PF00633; HHH; 1.
SUPFAM; SSF143597; SSF143597; 1.
SUPFAM; SSF47781; SSF47781; 1.
PROSITE; PS51794; DAC; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; DNA damage; DNA repair;
DNA-binding; Magnesium; Nucleotide-binding; Nucleotidyltransferase;
Reference proteome; Transferase.
CHAIN 1 357 DNA integrity scanning protein DisA.
/FTId=PRO_0000255653.
DOMAIN 8 148 DAC. {ECO:0000255|PROSITE-
ProRule:PRU01130}.
NP_BIND 107 111 ATP. {ECO:0000269|PubMed:18439896,
ECO:0000269|PubMed:26014055}.
NP_BIND 127 130 ATP. {ECO:0000269|PubMed:18439896,
ECO:0000269|PubMed:26014055}.
BINDING 76 76 ATP; via amide nitrogen.
{ECO:0000269|PubMed:18439896,
ECO:0000269|PubMed:26014055}.
BINDING 94 94 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:18439896,
ECO:0000269|PubMed:26014055}.
MUTAGEN 75 75 D->N: Significant loss of c-di-AMP
formation, still forms octamers.
{ECO:0000269|PubMed:26014055}.
MUTAGEN 107 111 TRHRT->VRHRV: Significant loss of c-di-
AMP formation.
{ECO:0000269|PubMed:26014055}.
MUTAGEN 108 110 RHR->AAA: About 90% loss of c-di-AMP
formation. {ECO:0000269|PubMed:26014055}.
MUTAGEN 128 130 RRR->AAA: 2-fold increase in c-di-AMP
formation. {ECO:0000269|PubMed:26014055}.
MUTAGEN 130 130 R->A: About 90% loss of c-di-AMP
formation. {ECO:0000269|PubMed:26014055}.
HELIX 9 15 {ECO:0000244|PDB:3C1Y}.
HELIX 16 18 {ECO:0000244|PDB:3C1Y}.
HELIX 23 33 {ECO:0000244|PDB:3C1Y}.
STRAND 38 42 {ECO:0000244|PDB:3C1Y}.
HELIX 46 49 {ECO:0000244|PDB:3C1Y}.
TURN 50 52 {ECO:0000244|PDB:3C1Y}.
STRAND 53 62 {ECO:0000244|PDB:3C1Y}.
HELIX 65 71 {ECO:0000244|PDB:3C1Y}.
STRAND 74 80 {ECO:0000244|PDB:3C1Y}.
STRAND 84 94 {ECO:0000244|PDB:3C1Y}.
HELIX 107 119 {ECO:0000244|PDB:3C1Y}.
STRAND 120 126 {ECO:0000244|PDB:3C1Y}.
STRAND 128 131 {ECO:0000244|PDB:3C1Z}.
STRAND 133 136 {ECO:0000244|PDB:3C1Y}.
STRAND 141 144 {ECO:0000244|PDB:3C1Y}.
HELIX 147 180 {ECO:0000244|PDB:3C1Y}.
HELIX 186 212 {ECO:0000244|PDB:3C1Y}.
HELIX 214 217 {ECO:0000244|PDB:3C1Y}.
HELIX 218 228 {ECO:0000244|PDB:3C1Y}.
HELIX 231 242 {ECO:0000244|PDB:3C1Y}.
STRAND 243 245 {ECO:0000244|PDB:3C1Y}.
HELIX 249 260 {ECO:0000244|PDB:3C1Y}.
STRAND 261 263 {ECO:0000244|PDB:3C23}.
HELIX 267 273 {ECO:0000244|PDB:3C1Y}.
HELIX 281 286 {ECO:0000244|PDB:3C1Y}.
HELIX 294 299 {ECO:0000244|PDB:3C1Y}.
HELIX 305 315 {ECO:0000244|PDB:3C1Y}.
HELIX 318 321 {ECO:0000244|PDB:3C1Y}.
HELIX 326 329 {ECO:0000244|PDB:3C1Y}.
HELIX 337 354 {ECO:0000244|PDB:3C1Y}.
SEQUENCE 357 AA; 40540 MW; 45C1318A21F315A9 CRC64;
MGVKSLVPQE LIEKIKLISP GTELRKALDD IINANFGALI FLVDDPKKYE DVIQGGFWLD
TDFSAEKLYE LSKMDGAIVL SEDITKIYYA NVHLVPDPTI PTGETGTRHR TAERLAKQTG
KVVIAVSRRR NIISLYYKNY KYVVNQVDFL ISKVTQAIST LEKYKDNFNK LLSELEVLEL
ENRVTLADVV RTLAKGFELL RIVEEIRPYI VELGEEGRLA RMQLRELTED VDDLLVLLIM
DYSSEEVEEE TAQNILQDFI TRREPSPISI SRVLGYDVQQ AAQLDDVLVS ARGYRLLKTV
ARIPLSIGYN VVRMFKTLDQ ISKASVEDLK KVEGIGEKRA RAISESISSL KHRKTSE


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