DACZ_HALVD
ID DACZ_HALVD Reviewed; 269 AA.
AC D4GZM5; L9VF24;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Diadenylate cyclase {ECO:0000255|HAMAP-Rule:MF_00840, ECO:0000303|PubMed:30884174};
DE Short=DAC {ECO:0000255|HAMAP-Rule:MF_00840, ECO:0000303|PubMed:30884174};
DE EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_00840, ECO:0000269|PubMed:30884174};
DE AltName: Full=Cyclic-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00840};
DE Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_00840};
GN Name=dacZ {ECO:0000255|HAMAP-Rule:MF_00840, ECO:0000303|PubMed:30884174};
GN OrderedLocusNames=HVO_1660 {ECO:0000312|EMBL:ADE04317.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, INDUCTION,
RP DISRUPTION PHENOTYPE, AND ROLE OF C-DI-AMP IN ARCHAEA.
RC STRAIN=H26;
RX PubMed=30884174; DOI=10.1002/mbo3.829;
RA Braun F., Thomalla L., van der Does C., Quax T.E.F., Allers T., Kaever V.,
RA Albers S.V.;
RT "Cyclic nucleotides in archaea: Cyclic di-AMP in the archaeon Haloferax
RT volcanii and its putative role.";
RL MicrobiologyOpen 2019:E829-E829(2019).
CC -!- FUNCTION: Diadenylate cyclase that catalyzes the condensation of 2 ATP
CC molecules into cyclic di-AMP (c-di-AMP). c-di-AMP is a second messenger
CC for intracellular signal transduction involved in the control of
CC important regulatory processes such as osmoregulation. Is essential for
CC H.volcanii. Overexpression of DacZ leads to cell death, suggesting the
CC need for tight regulation of c-di-AMP levels. Cannot use GTP as
CC substrate. {ECO:0000269|PubMed:30884174}.
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_00840,
CC ECO:0000269|PubMed:30884174};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:30884174};
CC Note=Cannot use Mg(2+), Ca(2+), Ni(2+) or Co(2+) instead of Mn(2+) as
CC cofactor. {ECO:0000269|PubMed:30884174};
CC -!- INDUCTION: Is constantly expressed at different growth phases in rich
CC and selective media. {ECO:0000269|PubMed:30884174}.
CC -!- DISRUPTION PHENOTYPE: It was not possible to obtain a strain in which
CC the dacZ gene was deleted in standard growth conditions, indicating
CC that dacZ is an essential gene. {ECO:0000269|PubMed:30884174}.
CC -!- SIMILARITY: Belongs to the adenylate cyclase family. DacZ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00840}.
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DR EMBL; CP001956; ADE04317.1; -; Genomic_DNA.
DR RefSeq; WP_004041551.1; NZ_AOHU01000029.1.
DR AlphaFoldDB; D4GZM5; -.
DR SMR; D4GZM5; -.
DR STRING; 309800.C498_03660; -.
DR EnsemblBacteria; ADE04317; ADE04317; HVO_1660.
DR GeneID; 8925157; -.
DR KEGG; hvo:HVO_1660; -.
DR PATRIC; fig|309800.29.peg.712; -.
DR eggNOG; arCOG04453; Archaea.
DR HOGENOM; CLU_063222_0_0_2; -.
DR OMA; TRDTNAI; -.
DR OrthoDB; 80301at2157; -.
DR BRENDA; 2.7.7.85; 2561.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106408; F:diadenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019932; P:second-messenger-mediated signaling; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1700.10; -; 1.
DR HAMAP; MF_00840; DacZ; 1.
DR InterPro; IPR014499; DAC_DacZ.
DR InterPro; IPR045586; DacZ_N.
DR InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR Pfam; PF02457; DAC; 1.
DR Pfam; PF19294; DUF5912; 1.
DR PIRSF; PIRSF019073; UCP019073; 1.
DR SUPFAM; SSF143597; SSF143597; 1.
DR PROSITE; PS51794; DAC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Manganese; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..269
FT /note="Diadenylate cyclase"
FT /id="PRO_0000447476"
FT DOMAIN 109..266
FT /note="DAC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00840"
SQ SEQUENCE 269 AA; 28953 MW; 0564D505AD414C79 CRC64;
MAALSELLGD LVADVDGLFL FTPSSSHYEQ FAETDVPTVV IAPENTVEAE TFVELPLQFQ
NVKDRIRFGV EGAMEQSIVE AGDTIACNVG TFGGDPDSLV RVRVEENMRS GIYDLFANSR
ADPGVIRDVF EVAIELGKKG QKGEPVGALF IVGDAGKVMN KSRPLSYNPF EKSHVYVGDP
IVNVMLKEFS RLDGAFVISD SGKIVSAYRY LEPSAEGVDI PKGLGARHMA GGAITRDTNA
TAIVLSESDG LVRAFKGGKM ILEIDPEAY
