DACA_LISMO
ID DACA_LISMO Reviewed; 273 AA.
AC Q8Y5E4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Diadenylate cyclase {ECO:0000255|HAMAP-Rule:MF_01499, ECO:0000303|PubMed:20508090};
DE Short=DAC {ECO:0000255|HAMAP-Rule:MF_01499};
DE EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_01499};
DE AltName: Full=Cyclic-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01499};
DE Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01499};
DE AltName: Full=Diadenylate cyclase CdaA {ECO:0000303|PubMed:25605729};
GN Name=dacA {ECO:0000255|HAMAP-Rule:MF_01499, ECO:0000303|PubMed:20508090};
GN Synonyms=cdaA {ECO:0000303|PubMed:25605729}; OrderedLocusNames=lmo2120;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP FUNCTION, GENE NAME, AND DISRUPTION PHENOTYPE.
RX PubMed=20508090; DOI=10.1126/science.1189801;
RA Woodward J.J., Iavarone A.T., Portnoy D.A.;
RT "c-di-AMP secreted by intracellular Listeria monocytogenes activates a host
RT type I interferon response.";
RL Science 328:1703-1705(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 101-273 IN COMPLEX WITH ATP,
RP FUNCTION, COFACTOR, SUBUNIT, AND MUTAGENESIS OF ASP-171; GLY-172 AND
RP THR-202.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=25605729; DOI=10.1074/jbc.m114.630418;
RA Rosenberg J., Dickmanns A., Neumann P., Gunka K., Arens J., Kaever V.,
RA Stuelke J., Ficner R., Commichau F.M.;
RT "Structural and biochemical analysis of the essential diadenylate cyclase
RT CdaA from Listeria monocytogenes.";
RL J. Biol. Chem. 290:6596-6606(2015).
CC -!- FUNCTION: Catalyzes the condensation of 2 ATP molecules into cyclic di-
CC AMP (c-di-AMP) (PubMed:25605729). c-di-AMP is a signaling compound
CC secreted into the host's cytosol where it triggers the cytosolic
CC surveillance pathway (CSP), a host pathway of innate immunity
CC characterized by expression of beta interferon (IFN-beta) and
CC coregulated genes (PubMed:20508090). Expression of truncated proteins
CC (missing first 80 or 100 residues) in E.coli leads to c-di-AMP
CC synthesis (PubMed:25605729). {ECO:0000269|PubMed:20508090,
CC ECO:0000269|PubMed:25605729}.
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_01499};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:25605729};
CC Note=Optimal activity at 0.5-1 mM CoCl(2), also functions with Mn(2+),
CC for a construct missing residues 1-80. {ECO:0000269|PubMed:25605729};
CC -!- SUBUNIT: Homodimer, required for active site formation (Probable).
CC {ECO:0000305|PubMed:25605729}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01499};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01499}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:20508090}.
CC -!- SIMILARITY: Belongs to the adenylate cyclase family. DacA/CdaA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01499}.
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DR EMBL; AL591982; CAD00198.1; -; Genomic_DNA.
DR PIR; AH1339; AH1339.
DR RefSeq; NP_465644.1; NC_003210.1.
DR RefSeq; WP_003722380.1; NZ_CP023861.1.
DR PDB; 4RV7; X-ray; 2.80 A; A/B/C/D=101-273.
DR PDB; 6HVL; X-ray; 2.80 A; A/B=101-273.
DR PDB; 6HVM; X-ray; 2.00 A; A/B=101-273.
DR PDB; 6HVN; X-ray; 2.23 A; A/B=101-273.
DR PDBsum; 4RV7; -.
DR PDBsum; 6HVL; -.
DR PDBsum; 6HVM; -.
DR PDBsum; 6HVN; -.
DR AlphaFoldDB; Q8Y5E4; -.
DR SMR; Q8Y5E4; -.
DR STRING; 169963.lmo2120; -.
DR PaxDb; Q8Y5E4; -.
DR EnsemblBacteria; CAD00198; CAD00198; CAD00198.
DR GeneID; 67410225; -.
DR GeneID; 984739; -.
DR KEGG; lmo:lmo2120; -.
DR PATRIC; fig|169963.11.peg.2172; -.
DR eggNOG; COG1624; Bacteria.
DR HOGENOM; CLU_038561_0_1_9; -.
DR OMA; ILWQGEL; -.
DR PhylomeDB; Q8Y5E4; -.
DR BioCyc; LMON169963:LMO2120-MON; -.
DR BRENDA; 2.7.7.85; 3045.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106408; F:diadenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:InterPro.
DR GO; GO:0019932; P:second-messenger-mediated signaling; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1700.10; -; 1.
DR HAMAP; MF_01499; DacA; 1.
DR InterPro; IPR014046; C-di-AMP_synthase.
DR InterPro; IPR034701; CdaA.
DR InterPro; IPR045585; CdaA_N.
DR InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR Pfam; PF19293; CdaA_N; 1.
DR Pfam; PF02457; DAC; 1.
DR PIRSF; PIRSF004793; UCP004793; 1.
DR SUPFAM; SSF143597; SSF143597; 1.
DR TIGRFAMs; TIGR00159; TIGR00159; 1.
DR PROSITE; PS51794; DAC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..273
FT /note="Diadenylate cyclase"
FT /id="PRO_0000424179"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01499"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01499"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01499"
FT DOMAIN 82..242
FT /note="DAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01130"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4RV7"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4RV7"
FT BINDING 201..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4RV7"
FT BINDING 222..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:4RV7"
FT MUTAGEN 171
FT /note="D->N: No c-di-AMP formation (construct without
FT residues 1-80)."
FT /evidence="ECO:0000269|PubMed:25605729"
FT MUTAGEN 172
FT /note="G->A: No c-di-AMP formation (construct without
FT residues 1-80)."
FT /evidence="ECO:0000269|PubMed:25605729"
FT MUTAGEN 202
FT /note="T->N: No c-di-AMP formation (construct without
FT residues 1-80)."
FT /evidence="ECO:0000269|PubMed:25605729"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6HVL"
FT HELIX 105..125
FT /evidence="ECO:0007829|PDB:6HVM"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6HVM"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:4RV7"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:6HVM"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:6HVM"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:6HVM"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:6HVM"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:6HVM"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:6HVM"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:6HVM"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6HVM"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:6HVM"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:6HVM"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:6HVM"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:6HVM"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:6HVN"
SQ 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
