DACB_MYCGE
ID DACB_MYCGE Reviewed; 200 AA.
AC P47351;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Diadenylate cyclase {ECO:0000255|HAMAP-Rule:MF_00838};
DE Short=DAC {ECO:0000255|HAMAP-Rule:MF_00838};
DE EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_00838};
DE AltName: Full=Cyclic-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00838};
DE Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00838};
DE AltName: Full=Diadenylyl cyclase {ECO:0000303|PubMed:23812326};
GN Name=dacB {ECO:0000255|HAMAP-Rule:MF_00838, ECO:0000303|PubMed:23812326};
GN OrderedLocusNames=MG105;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP GENE NAME.
RX PubMed=23812326; DOI=10.1038/nrmicro3069;
RA Corrigan R.M., Gruendling A.;
RT "Cyclic di-AMP: another second messenger enters the fray.";
RL Nat. Rev. Microbiol. 11:513-524(2013).
RN [3]
RP SEQUENCE REVISION TO 84, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=16407165; DOI=10.1073/pnas.0510013103;
RA Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R.,
RA Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.;
RT "Essential genes of a minimal bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:425-430(2006).
CC -!- FUNCTION: Catalyzes the condensation of 2 ATP molecules into cyclic di-
CC AMP (c-di-AMP), a second messenger used to regulate differing processes
CC in different bacteria. {ECO:0000255|HAMAP-Rule:MF_00838}.
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_00838};
CC -!- SUBUNIT: Probably oligomerizes. {ECO:0000255|HAMAP-Rule:MF_00838}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00838};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00838}.
CC -!- DISRUPTION PHENOTYPE: Probably essential, it was not disrupted in a
CC global transposon mutagenesis study. {ECO:0000269|PubMed:16407165}.
CC -!- SIMILARITY: Belongs to the adenylate cyclase family. DacB/CdaS
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00838}.
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DR EMBL; L43967; AAC71323.2; -; Genomic_DNA.
DR PIR; F64211; F64211.
DR RefSeq; WP_009885663.1; NZ_AAGX01000002.1.
DR AlphaFoldDB; P47351; -.
DR SMR; P47351; -.
DR STRING; 243273.MG_105; -.
DR PRIDE; P47351; -.
DR EnsemblBacteria; AAC71323; AAC71323; MG_105.
DR KEGG; mge:MG_105; -.
DR eggNOG; COG1624; Bacteria.
DR HOGENOM; CLU_038561_2_0_14; -.
DR OMA; YAATFYK; -.
DR OrthoDB; 1300262at2; -.
DR Proteomes; UP000000807; 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; IBA:GO_Central.
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_00838; DacB; 1.
DR InterPro; IPR014046; C-di-AMP_synthase.
DR InterPro; IPR034701; CdaA.
DR InterPro; IPR034693; CdaS.
DR InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR InterPro; IPR003390; DNA_integrity_scan_DisA_N.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..200
FT /note="Diadenylate cyclase"
FT /id="PRO_0000210417"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00838"
FT DOMAIN 28..185
FT /note="DAC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00838"
SQ SEQUENCE 200 AA; 22654 MW; F8142E5962B77E60 CRC64;
MVVNILLFIT LIFLLLLFVF LIAFAFLNKR VRNYVVRTWT SVFSKSKQNL DKKNFFDNLT
STLLRLSVDK IGAIIAIEKR DSLDPYINIG YRVSSDFSPE LLVTIFYNKS SPLHDGAVIV
RDYKIISVSS YFPMTRQLID VSYGSRHRSA LGLSEKSDAV VFIVSETTGK ISVALKGVIK
TLSSNSDRLQ DEIIHYLSSK
