(data stored in SCRATCH zone)

SWISSPROT: D6XWS0_BACIE

ID   D6XWS0_BACIE            Unreviewed;       272 AA.
AC   D6XWS0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 56.
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=Bsel_0372 {ECO:0000313|EMBL:ADH97912.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97912.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97912.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001791; ADH97912.1; -; Genomic_DNA.
DR   RefSeq; WP_013171341.1; NC_014219.1.
DR   STRING; 439292.Bsel_0372; -.
DR   EnsemblBacteria; ADH97912; ADH97912; Bsel_0372.
DR   KEGG; bse:Bsel_0372; -.
DR   eggNOG; ENOG4105C8B; Bacteria.
DR   eggNOG; COG1624; LUCA.
DR   HOGENOM; HOG000054800; -.
DR   KO; K18672; -.
DR   OMA; ILWQGEL; -.
DR   OrthoDB; 1300262at2; -.
DR   BioCyc; BSEL439292:G1GLR-402-MONOMER; -.
DR   Proteomes; UP000000271; 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; D6XWS0.
DR   SWISS-2DPAGE; D6XWS0.
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:UP000000271};
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:UP000000271};
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      6     27       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01499}.
FT   TRANSMEM     39     57       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01499}.
FT   TRANSMEM     63     80       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01499}.
FT   DOMAIN       81    241       DAC. {ECO:0000259|PROSITE:PS51794}.
SQ   SEQUENCE   272 AA;  30498 MW;  D9BAB5407B34484F CRC64;
     MFEDLTFWRL VAIVVDITLV AFVIYKLIMV IRGTRAVQLV KGITVILTVW FLSGYFGLHT
     LQWLMQQAVI YGVLAIIIIF QPELRRALEH LGRGKLFQSS STANAEEIEE MIEHLIKSTN
     YMGKRRIGAL ISIERETGMN DYIETGVKLN ANLTTELMTN IFIPNAPLHD GAVVLQNGSI
     AAAGCYLPLS ENPFISKELG TRHRAALGVS EVTDALTLVV SEETGAISMT KNGELHRNLD
     QDHLRKMLEK ELMNKEEDKG TSRWQWGGRN NG
//

If you have problems or comments...

PBIL Back to PBIL home page