(data stored in SCRATCH zone)

SWISSPROT: CDAA_BACSU

ID   CDAA_BACSU              Reviewed;         273 AA.
AC   Q45589; Q45590; Q7DL98;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   11-DEC-2019, entry version 108.
DE   RecName: Full=Cyclic di-AMP synthase CdaA {ECO:0000303|PubMed:22211522, ECO:0000303|PubMed:23192352};
DE            Short=c-di-AMP synthase;
DE            EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_01499};
DE   AltName: Full=Diadenylate cyclase;
DE            Short=DAC {ECO:0000255|HAMAP-Rule:MF_01499};
GN   Name=cdaA {ECO:0000303|PubMed:23192352}; Synonyms=ybbP;
GN   OrderedLocusNames=BSU01750;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9274029; DOI=10.1099/00221287-143-8-2763;
RA   Liu H., Haga K., Yasumoto K., Ohashi Y., Yoshikawa H., Takahashi H.;
RT   "Sequence and analysis of a 31 kb segment of the Bacillus subtilis
RT   chromosome in the area of the rrnH and rrnG operons.";
RL   Microbiology 143:2763-2767(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 270.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   PROBABLE FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=22211522; DOI=10.1111/j.1365-2958.2011.07953.x;
RA   Luo Y., Helmann J.D.;
RT   "Analysis of the role of Bacillus subtilis sigma(M) in beta-lactam
RT   resistance reveals an essential role for c-di-AMP in peptidoglycan
RT   homeostasis.";
RL   Mol. Microbiol. 83:623-639(2012).
RN   [5]
RP   FUNCTION, ACTIVITY REGULATION, INTERACTION WITH CDAR, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23192352; DOI=10.1074/jbc.m112.395491;
RA   Mehne F.M., Gunka K., Eilers H., Herzberg C., Kaever V., Stuelke J.;
RT   "Cyclic di-AMP homeostasis in Bacillus subtilis: both lack and high level
RT   accumulation of the nucleotide are detrimental for cell growth.";
RL   J. Biol. Chem. 288:2004-2017(2013).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=168, and 168 / YB886 / BG214;
RX   PubMed=25616256; DOI=10.1016/j.dnarep.2014.12.007;
RA   Gandara C., Alonso J.C.;
RT   "DisA and c-di-AMP act at the intersection between DNA-damage response and
RT   stress homeostasis in exponentially growing Bacillus subtilis cells.";
RL   DNA Repair 27:1-8(2015).
RN   [7]
RP   FUNCTION, SUBUNIT, INTERACTION WITH CDAR, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=26240071; DOI=10.1128/jb.00564-15;
RA   Gundlach J., Mehne F.M., Herzberg C., Kampf J., Valerius O., Kaever V.,
RA   Stuelke J.;
RT   "An essential poison: synthesis and degradation of cyclic di-AMP in
RT   Bacillus subtilis.";
RL   J. Bacteriol. 197:3265-3274(2015).
CC   -!- FUNCTION: One of 3 paralogous diadenylate cyclases (DAC) in this
CC       bacteria, catalyzing the condensation of 2 ATP molecules into cyclic
CC       di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di-
CC       AMP synthesis (PubMed:23192352). Probably the main producer of c-di-AMP
CC       for the cell; is probably implicated in control of peptidogylcan
CC       synthesis (PubMed:22211522, PubMed:23192352, PubMed:26240071). In
CC       B.subtilis c-di-AMP is a second messenger that mediates growth, DNA
CC       repair and cell wall homeostasis; it is toxic when present in excess
CC       (PubMed:26240071). {ECO:0000269|PubMed:23192352,
CC       ECO:0000269|PubMed:26240071, ECO:0000305|PubMed:22211522}.
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   -!- ACTIVITY REGULATION: DAC activity is stimulated about 20-fold in E.coli
CC       by coexpression with CdaR (PubMed:23192352).
CC       {ECO:0000269|PubMed:23192352}.
CC   -!- SUBUNIT: Probably a homodimer (By similarity). Interacts with CdaR
CC       (PubMed:23192352, PubMed:26240071). May interact with GlmM
CC       (PubMed:26240071). {ECO:0000255|HAMAP-Rule:MF_01499,
CC       ECO:0000269|PubMed:23192352, ECO:0000269|PubMed:26240071}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01499,
CC       ECO:0000269|PubMed:26240071}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01499}.
CC   -!- INDUCTION: Constitutively expressed, part of the cdaA-cdaR-glmM-glmS
CC       operon (PubMed:23192352). {ECO:0000269|PubMed:23192352}.
CC   -!- DISRUPTION PHENOTYPE: Increased sensitivity to the beta-lactam
CC       antibiotic cefuroxime (CEF), upon overexpression of the c-di-AMP
CC       phosphodiesterase GdpP greatly increased sensitivity to CEF
CC       (PubMed:22211522). Double disA-cdaA mutants cannot be made, suggesting
CC       they are lethal, while double disA-cdaS and cdaA-cdaS mutants are
CC       viable (PubMed:22211522, PubMed:23192352). Depletion of cdaA in double
CC       disA-cdaA deletion cells leads to cell lysis (PubMed:22211522).
CC       Exponentially growing cells are extremely sensitive to H(2)O(2), no
CC       change in response to methyl methanesulfonate (PubMed:25616256).
CC       {ECO:0000269|PubMed:22211522, ECO:0000269|PubMed:23192352,
CC       ECO:0000269|PubMed:25616256}.
CC   -!- SIMILARITY: Belongs to the adenylate cyclase family. DacA/CdaA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01499}.
DR   EMBL; AB002150; BAA19509.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11951.2; -; Genomic_DNA.
DR   PIR; H69744; H69744.
DR   RefSeq; NP_388056.2; NC_000964.3.
DR   RefSeq; WP_003223651.1; NZ_JNCM01000030.1.
DR   SMR; Q45589; -.
DR   STRING; 224308.BSU01750; -.
DR   PaxDb; Q45589; -.
DR   PRIDE; Q45589; -.
DR   EnsemblBacteria; CAB11951; CAB11951; BSU01750.
DR   GeneID; 938735; -.
DR   KEGG; bsu:BSU01750; -.
DR   PATRIC; fig|224308.179.peg.181; -.
DR   eggNOG; ENOG4105C8B; Bacteria.
DR   eggNOG; COG1624; LUCA.
DR   HOGENOM; HOG000054800; -.
DR   InParanoid; Q45589; -.
DR   KO; K18672; -.
DR   OMA; ILWQGEL; -.
DR   PhylomeDB; Q45589; -.
DR   BioCyc; BSUB:BSU01750-MONOMER; -.
DR   PRO; PR:Q45589; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
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   1: Evidence at protein level;
DR   PRODOM; Q45589.
DR   SWISS-2DPAGE; Q45589.
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..273
FT                   /note="Cyclic di-AMP synthase CdaA"
FT                   /id="PRO_0000360441"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01499"
FT   TRANSMEM        40..60
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   CONFLICT        270
FT                   /note="K -> R (in Ref. 1; BAA19509)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   273 AA;  30547 MW;  29F2984C5F90007C CRC64;
     MAFEDIPFLQ YLGNAVDILL VWYVIYKLIM VIRGTKAVQL LKGIVVIVLV RMASQYLGLS
     TLQWLMDQAI TWGFLAIIII FQPELRRALE QLGRGRFFSR SGTPVEEAQQ KTIEAITKAI
     NYMAKRRIGA LLTIERDTGM GDYIETGIPL NAKVSSELLI NIFIPNTPLH DGAVIMKNNE
     IAAAACYLPL SESPFISKEL GTRHRAAVGI SEVTDSLTII VSEETGGVSV AKNGDLHREL
     TEEALKEMLE AEFKKNTRDT SSNRWYWRGK KNG
//

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