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Diadenylate cyclase (DAC) (EC 2.7.7.85) (Cyclic-di-AMP synthase) (c-di-AMP synthase) (Diadenylate cyclase CdaA)

 DACA_LISMO              Reviewed;         273 AA.
Q8Y5E4;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
20-JUN-2018, entry version 83.
RecName: Full=Diadenylate cyclase {ECO:0000255|HAMAP-Rule:MF_01499, ECO:0000303|PubMed:20508090};
Short=DAC {ECO:0000255|HAMAP-Rule:MF_01499};
EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_01499};
AltName: Full=Cyclic-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01499};
Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01499};
AltName: Full=Diadenylate cyclase CdaA {ECO:0000303|PubMed:25605729};
Name=dacA {ECO:0000255|HAMAP-Rule:MF_01499,
ECO:0000303|PubMed:20508090};
Synonyms=cdaA {ECO:0000303|PubMed:25605729};
OrderedLocusNames=lmo2120;
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
NCBI_TaxID=169963;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-679 / EGD-e;
PubMed=11679669; DOI=10.1126/science.1063447;
Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
"Comparative genomics of Listeria species.";
Science 294:849-852(2001).
[2]
FUNCTION, GENE NAME, AND DISRUPTION PHENOTYPE.
PubMed=20508090; DOI=10.1126/science.1189801;
Woodward J.J., Iavarone A.T., Portnoy D.A.;
"c-di-AMP secreted by intracellular Listeria monocytogenes activates a
host type I interferon response.";
Science 328:1703-1705(2010).
[3]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 101-273 IN COMPLEX WITH ATP,
FUNCTION, COFACTOR, SUBUNIT, AND MUTAGENESIS OF ASP-171; GLY-172 AND
THR-202.
STRAIN=ATCC BAA-679 / EGD-e;
PubMed=25605729; DOI=10.1074/jbc.M114.630418;
Rosenberg J., Dickmanns A., Neumann P., Gunka K., Arens J., Kaever V.,
Stuelke J., Ficner R., Commichau F.M.;
"Structural and biochemical analysis of the essential diadenylate
cyclase CdaA from Listeria monocytogenes.";
J. Biol. Chem. 290:6596-6606(2015).
-!- FUNCTION: Catalyzes the condensation of 2 ATP molecules into
cyclic di-AMP (c-di-AMP) (PubMed:25605729). c-di-AMP is a
signaling compound secreted into the host's cytosol where it
triggers the cytosolic surveillance pathway (CSP), a host pathway
of innate immunity characterized by expression of beta interferon
(IFN-beta) and coregulated genes (PubMed:20508090). Expression of
truncated proteins (missing first 80 or 100 residues) in E.coli
leads to c-di-AMP synthesis (PubMed:25605729).
{ECO:0000269|PubMed:20508090, ECO:0000269|PubMed:25605729}.
-!- CATALYTIC ACTIVITY: 2 ATP = 2 diphosphate + cyclic di-3',5'-
adenylate. {ECO:0000255|HAMAP-Rule:MF_01499}.
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:25605729};
Note=Optimal activity at 0.5-1 mM CoCl(2), also functions with
Mn(2+), for a construct missing residues 1-80.
{ECO:0000269|PubMed:25605729};
-!- SUBUNIT: Homodimer, required for active site formation (Probable).
{ECO:0000305|PubMed:25605729}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
Rule:MF_01499}; Multi-pass membrane protein {ECO:0000255|HAMAP-
Rule:MF_01499}.
-!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
{ECO:0000269|PubMed:20508090}.
-!- SIMILARITY: Belongs to the adenylate cyclase family. DacA/CdaA
subfamily. {ECO:0000255|HAMAP-Rule:MF_01499}.
-----------------------------------------------------------------------
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EMBL; AL591982; CAD00198.1; -; Genomic_DNA.
PIR; AH1339; AH1339.
RefSeq; NP_465644.1; NC_003210.1.
RefSeq; WP_003722380.1; NC_003210.1.
PDB; 4RV7; X-ray; 2.80 A; A/B/C/D=101-273.
PDBsum; 4RV7; -.
ProteinModelPortal; Q8Y5E4; -.
SMR; Q8Y5E4; -.
STRING; 169963.lmo2120; -.
PaxDb; Q8Y5E4; -.
PRIDE; Q8Y5E4; -.
EnsemblBacteria; CAD00198; CAD00198; CAD00198.
GeneID; 984739; -.
KEGG; lmo:lmo2120; -.
PATRIC; fig|169963.11.peg.2172; -.
eggNOG; ENOG4105C8B; Bacteria.
eggNOG; COG1624; LUCA.
HOGENOM; HOG000054800; -.
KO; K18672; -.
OMA; ILWQGEL; -.
PhylomeDB; Q8Y5E4; -.
BioCyc; LMON169963:LMO2120-MONOMER; -.
BRENDA; 2.7.7.85; 3045.
Proteomes; UP000000817; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
Gene3D; 3.40.1700.10; -; 1.
HAMAP; MF_01499; DacA; 1.
InterPro; IPR014046; c-di-AMP_synthase.
InterPro; IPR034701; CdaA.
InterPro; IPR036888; DNA_integrity_DisA_N_sf.
InterPro; IPR003390; DNA_integrity_scan_DisA_N.
Pfam; PF02457; DisA_N; 1.
PIRSF; PIRSF004793; UCP004793; 1.
SUPFAM; SSF143597; SSF143597; 1.
TIGRFAMs; TIGR00159; TIGR00159; 1.
PROSITE; PS51794; DAC; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell membrane; Complete proteome; Membrane;
Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 273 Diadenylate cyclase.
/FTId=PRO_0000424179.
TRANSMEM 12 32 Helical. {ECO:0000255|HAMAP-
Rule:MF_01499}.
TRANSMEM 37 57 Helical. {ECO:0000255|HAMAP-
Rule:MF_01499}.
TRANSMEM 61 81 Helical. {ECO:0000255|HAMAP-
Rule:MF_01499}.
DOMAIN 82 242 DAC. {ECO:0000255|PROSITE-
ProRule:PRU01130}.
NP_BIND 201 204 ATP. {ECO:0000244|PDB:4RV7}.
NP_BIND 222 224 ATP. {ECO:0000244|PDB:4RV7}.
BINDING 171 171 ATP. {ECO:0000244|PDB:4RV7}.
BINDING 188 188 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000244|PDB:4RV7}.
MUTAGEN 171 171 D->N: No c-di-AMP formation (construct
without residues 1-80).
{ECO:0000269|PubMed:25605729}.
MUTAGEN 172 172 G->A: No c-di-AMP formation (construct
without residues 1-80).
{ECO:0000269|PubMed:25605729}.
MUTAGEN 202 202 T->N: No c-di-AMP formation (construct
without residues 1-80).
{ECO:0000269|PubMed:25605729}.
HELIX 101 126 {ECO:0000244|PDB:4RV7}.
STRAND 130 134 {ECO:0000244|PDB:4RV7}.
STRAND 136 139 {ECO:0000244|PDB:4RV7}.
HELIX 141 144 {ECO:0000244|PDB:4RV7}.
STRAND 147 153 {ECO:0000244|PDB:4RV7}.
HELIX 156 162 {ECO:0000244|PDB:4RV7}.
HELIX 168 170 {ECO:0000244|PDB:4RV7}.
STRAND 171 177 {ECO:0000244|PDB:4RV7}.
STRAND 180 186 {ECO:0000244|PDB:4RV7}.
HELIX 202 213 {ECO:0000244|PDB:4RV7}.
STRAND 217 221 {ECO:0000244|PDB:4RV7}.
TURN 223 225 {ECO:0000244|PDB:4RV7}.
STRAND 228 232 {ECO:0000244|PDB:4RV7}.
STRAND 235 237 {ECO:0000244|PDB:4RV7}.
HELIX 242 253 {ECO:0000244|PDB:4RV7}.
SEQUENCE 273 AA; 30445 MW; 878951A75FB06D88 CRC64;
MDFSNMSILH YLANIVDILV VWFVIYKVIM LIRGTKAVQL LKGIFIIIAV KLLSGFFGLQ
TVEWITDQML TWGFLAIIII FQPELRRALE TLGRGNIFTR YGSRIEREQH HLIESIEKST
QYMAKRRIGA LISVARDTGM DDYIETGIPL NAKISSQLLI NIFIPNTPLH DGAVIIKGNE
IASAASYLPL SDSPFLSKEL GTRHRAALGI SEVTDSITIV VSEETGGISL TKGGELFRDV
SEEELHKILL KELVTVTAKK PSIFSKWKGG KSE


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