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Cyclic di-AMP synthase CdaA (c-di-AMP synthase) (EC 2.7.7.85) (Diadenylate cyclase) (DAC)

 CDAA_BACSU              Reviewed;         273 AA.
Q45589; Q45590; Q7DL98;
20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 3.
25-OCT-2017, entry version 98.
RecName: Full=Cyclic di-AMP synthase CdaA {ECO:0000303|PubMed:22211522, ECO:0000303|PubMed:23192352};
Short=c-di-AMP synthase;
EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_01499};
AltName: Full=Diadenylate cyclase;
Short=DAC {ECO:0000255|HAMAP-Rule:MF_01499};
Name=cdaA {ECO:0000303|PubMed:23192352}; Synonyms=ybbP;
OrderedLocusNames=BSU01750;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9274029; DOI=10.1099/00221287-143-8-2763;
Liu H., Haga K., Yasumoto K., Ohashi Y., Yoshikawa H., Takahashi H.;
"Sequence and analysis of a 31 kb segment of the Bacillus subtilis
chromosome in the area of the rrnH and rrnG operons.";
Microbiology 143:2763-2767(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
SEQUENCE REVISION TO 270.
PubMed=19383706; DOI=10.1099/mic.0.027839-0;
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
"From a consortium sequence to a unified sequence: the Bacillus
subtilis 168 reference genome a decade later.";
Microbiology 155:1758-1775(2009).
[4]
PROBABLE FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=168;
PubMed=22211522; DOI=10.1111/j.1365-2958.2011.07953.x;
Luo Y., Helmann J.D.;
"Analysis of the role of Bacillus subtilis sigma(M) in beta-lactam
resistance reveals an essential role for c-di-AMP in peptidoglycan
homeostasis.";
Mol. Microbiol. 83:623-639(2012).
[5]
FUNCTION, ENZYME REGULATION, INTERACTION WITH CDAR, INDUCTION, AND
DISRUPTION PHENOTYPE.
PubMed=23192352; DOI=10.1074/jbc.M112.395491;
Mehne F.M., Gunka K., Eilers H., Herzberg C., Kaever V., Stuelke J.;
"Cyclic di-AMP homeostasis in Bacillus subtilis: both lack and high
level accumulation of the nucleotide are detrimental for cell
growth.";
J. Biol. Chem. 288:2004-2017(2013).
[6]
DISRUPTION PHENOTYPE.
STRAIN=168, and 168 / YB886 / BG214;
PubMed=25616256; DOI=10.1016/j.dnarep.2014.12.007;
Gandara C., Alonso J.C.;
"DisA and c-di-AMP act at the intersection between DNA-damage response
and stress homeostasis in exponentially growing Bacillus subtilis
cells.";
DNA Repair 27:1-8(2015).
[7]
FUNCTION, SUBUNIT, INTERACTION WITH CDAR, AND SUBCELLULAR LOCATION.
STRAIN=168;
PubMed=26240071; DOI=10.1128/JB.00564-15;
Gundlach J., Mehne F.M., Herzberg C., Kampf J., Valerius O.,
Kaever V., Stuelke J.;
"An essential poison: synthesis and degradation of cyclic di-AMP in
Bacillus subtilis.";
J. Bacteriol. 197:3265-3274(2015).
-!- FUNCTION: One of 3 paralogous diadenylate cyclases (DAC) in this
bacteria, catalyzing the condensation of 2 ATP molecules into
cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli
leads to c-di-AMP synthesis (PubMed:23192352). Probably the main
producer of c-di-AMP for the cell; is probably implicated in
control of peptidogylcan synthesis (PubMed:22211522,
PubMed:23192352, PubMed:26240071). In B.subtilis c-di-AMP is a
second messenger that mediates growth, DNA repair and cell wall
homeostasis; it is toxic when present in excess (PubMed:26240071).
{ECO:0000269|PubMed:23192352, ECO:0000269|PubMed:26240071,
ECO:0000305|PubMed:22211522}.
-!- CATALYTIC ACTIVITY: 2 ATP = 2 diphosphate + cyclic di-3',5'-
adenylate. {ECO:0000255|HAMAP-Rule:MF_01499}.
-!- ENZYME REGULATION: DAC activity is stimulated about 20-fold in
E.coli by coexpression with CdaR (PubMed:23192352).
{ECO:0000269|PubMed:23192352}.
-!- SUBUNIT: Probably a homodimer (By similarity). Interacts with CdaR
(PubMed:23192352, PubMed:26240071). May interact with GlmM
(PubMed:26240071). {ECO:0000255|HAMAP-Rule:MF_01499,
ECO:0000269|PubMed:23192352, ECO:0000269|PubMed:26240071}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
Rule:MF_01499, ECO:0000269|PubMed:26240071}; Multi-pass membrane
protein {ECO:0000255|HAMAP-Rule:MF_01499}.
-!- INDUCTION: Constitutively expressed, part of the cdaA-cdaR-glmM-
glmS operon (PubMed:23192352). {ECO:0000269|PubMed:23192352}.
-!- DISRUPTION PHENOTYPE: Increased sensitivity to the beta-lactam
antibiotic cefuroxime (CEF), upon overexpression of the c-di-AMP
phosphodiesterase GdpP greatly increased sensitivity to CEF
(PubMed:22211522). Double disA-cdaA mutants cannot be made,
suggesting they are lethal, while double disA-cdaS and cdaA-cdaS
mutants are viable (PubMed:22211522, PubMed:23192352). Depletion
of cdaA in double disA-cdaA deletion cells leads to cell lysis
(PubMed:22211522). Exponentially growing cells are extremely
sensitive to H(2)O(2), no change in response to methyl
methanesulfonate (PubMed:25616256). {ECO:0000269|PubMed:22211522,
ECO:0000269|PubMed:23192352, ECO:0000269|PubMed:25616256}.
-!- SIMILARITY: Belongs to the adenylate cyclase family. DacA/CdaA
subfamily. {ECO:0000255|HAMAP-Rule:MF_01499}.
-----------------------------------------------------------------------
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EMBL; AB002150; BAA19509.1; -; Genomic_DNA.
EMBL; AL009126; CAB11951.2; -; Genomic_DNA.
PIR; H69744; H69744.
RefSeq; NP_388056.2; NC_000964.3.
RefSeq; WP_003223651.1; NZ_JNCM01000030.1.
ProteinModelPortal; Q45589; -.
SMR; Q45589; -.
STRING; 224308.Bsubs1_010100000998; -.
PaxDb; Q45589; -.
PRIDE; Q45589; -.
EnsemblBacteria; CAB11951; CAB11951; BSU01750.
GeneID; 938735; -.
KEGG; bsu:BSU01750; -.
PATRIC; fig|224308.179.peg.181; -.
eggNOG; ENOG4105C8B; Bacteria.
eggNOG; COG1624; LUCA.
HOGENOM; HOG000054800; -.
InParanoid; Q45589; -.
KO; K18672; -.
OMA; ILWQGEL; -.
PhylomeDB; Q45589; -.
BioCyc; BSUB:BSU01750-MONOMER; -.
PRO; PR:Q45589; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
Gene3D; 3.40.1700.10; -; 1.
HAMAP; MF_01499; DacA; 1.
InterPro; IPR014046; c-di-AMP_synthase.
InterPro; IPR034701; CdaA.
InterPro; IPR036888; DNA_integrity_DisA_N_sf.
InterPro; IPR003390; DNA_integrity_scan_DisA_N.
Pfam; PF02457; DisA_N; 1.
PIRSF; PIRSF004793; UCP004793; 1.
SUPFAM; SSF143597; SSF143597; 1.
TIGRFAMs; TIGR00159; TIGR00159; 1.
PROSITE; PS51794; DAC; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Membrane;
Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 273 Cyclic di-AMP synthase CdaA.
/FTId=PRO_0000360441.
TRANSMEM 12 32 Helical. {ECO:0000255|HAMAP-
Rule:MF_01499}.
TRANSMEM 40 60 Helical. {ECO:0000255|HAMAP-
Rule:MF_01499}.
TRANSMEM 61 81 Helical. {ECO:0000255|HAMAP-
Rule:MF_01499}.
DOMAIN 82 242 DAC. {ECO:0000255|PROSITE-
ProRule:PRU01130}.
CONFLICT 270 270 K -> R (in Ref. 1; BAA19509).
{ECO:0000305}.
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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