(data stored in SCRATCH zone)

SWISSPROT: C8W669_DESAS

ID   C8W669_DESAS            Unreviewed;       275 AA.
AC   C8W669;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 48.
DE   RecName: Full=Diadenylate cyclase {ECO:0000256|HAMAP-Rule:MF_01499};
DE            Short=DAC {ECO:0000256|HAMAP-Rule:MF_01499};
DE            EC=2.7.7.85 {ECO:0000256|HAMAP-Rule:MF_01499};
DE   AltName: Full=Cyclic-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_01499};
DE            Short=c-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_01499};
GN   Name=dacA {ECO:0000256|HAMAP-Rule:MF_01499};
GN   OrderedLocusNames=Dtox_0604 {ECO:0000313|EMBL:ACV61524.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61524.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61524.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Catalyzes the condensation of 2 ATP molecules into
CC       cyclic di-AMP (c-di-AMP), a second messenger used to regulate
CC       differing processes in different bacteria. {ECO:0000256|HAMAP-
CC       Rule:MF_01499}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP = c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500;
CC         EC=2.7.7.85; Evidence={ECO:0000256|HAMAP-Rule:MF_01499,
CC         ECO:0000256|SAAS:SAAS01115408};
CC   -!- SUBUNIT: Probably a homodimer. {ECO:0000256|HAMAP-Rule:MF_01499}.
CC   -!- SIMILARITY: Belongs to the adenylate cyclase family. DacA/CdaA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01499}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01499}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001720; ACV61524.1; -; Genomic_DNA.
DR   RefSeq; WP_015756243.1; NC_013216.1.
DR   STRING; 485916.Dtox_0604; -.
DR   EnsemblBacteria; ACV61524; ACV61524; Dtox_0604.
DR   KEGG; dae:Dtox_0604; -.
DR   eggNOG; ENOG4105C8B; Bacteria.
DR   eggNOG; COG1624; LUCA.
DR   HOGENOM; HOG000054800; -.
DR   KO; K18672; -.
DR   OMA; ILWQGEL; -.
DR   OrthoDB; 1300262at2; -.
DR   BioCyc; DACE485916:G1GFV-610-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
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; IPR036888; DNA_integrity_DisA_N_sf.
DR   InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR   Pfam; PF02457; DisA_N; 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;
DR   PRODOM; C8W669.
DR   SWISS-2DPAGE; C8W669.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01499,
KW   ECO:0000256|SAAS:SAAS00772210};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01499};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01499};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01499,
KW   ECO:0000256|SAAS:SAAS00772222};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01499,
KW   ECO:0000256|SAAS:SAAS00772249};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01499,
KW   ECO:0000256|SAAS:SAAS00772224};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01499};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01499}.
FT   TRANSMEM     14     34       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01499}.
FT   TRANSMEM     46     64       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01499}.
FT   DOMAIN       88    249       DAC. {ECO:0000259|PROSITE:PS51794}.
SQ   SEQUENCE   275 AA;  30044 MW;  6B69205C91F335F7 CRC64;
     MDFSQLIKLG LPRISFSVTT LIDLMIVAFV VYRIYLLIKG TRAVQLIKGL IVLVVAMVVS
     DWIHLNTVNW LLRQAVTGLI VALPVVFQPE LRRGLEKLGG GRFLARNVFM LAEEEKNTMI
     REVVRAVQML AKNSIGALIV LERGTGLEEY VDTGTKIDGE ISAELLVNIF IPKTPLHDGA
     VVVRGDRILA AACVLPLDES PNVNKALGTR HRAALGISEQ SDAMAVIVSE ETGVISLAVE
     GGLIRYLDDI SLAENLNKGL GGSTKLKFST LWKFK
//

If you have problems or comments...

PBIL Back to PBIL home page