(data stored in ACNUC7421 zone)

SWISSPROT: DARA_BACSU

ID   DARA_BACSU              Reviewed;         109 AA.
AC   P37538;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 97.
DE   RecName: Full=Cyclic di-AMP receptor A {ECO:0000303|PubMed:25433025};
DE            Short=c-di-AMP receptor A {ECO:0000303|PubMed:25433025};
DE   AltName: Full=PII-like signal transduction protein DarA {ECO:0000303|PubMed:25433025};
GN   Name=darA {ECO:0000303|PubMed:25433025}; Synonyms=yaaQ;
GN   OrderedLocusNames=BSU00290;
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=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
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] {ECO:0000244|PDB:4RLE}
RP   X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH C-DI-AMP, FUNCTION,
RP   SUBUNIT, DOMAIN, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=25433025; DOI=10.1074/jbc.m114.619619;
RA   Gundlach J., Dickmanns A., Schroder-Tittmann K., Neumann P., Kaesler J.,
RA   Kampf J., Herzberg C., Hammer E., Schwede F., Kaever V., Tittmann K.,
RA   Stulke J., Ficner R.;
RT   "Identification, characterization, and structure analysis of the cyclic di-
RT   AMP-binding PII-like signal transduction protein DarA.";
RL   J. Biol. Chem. 290:3069-3080(2015).
CC   -!- FUNCTION: Binds cyclic di-AMP (c-di-AMP) and is probably involved in c-
CC       di-AMP-mediated signaling pathways. In vitro, can also bind cyclic GMP-
CC       AMP (3'3'-cGAMP), with lower affinity, but not c-di-GMP or 2'3'-cGAMP.
CC       {ECO:0000269|PubMed:25433025}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:25433025}.
CC   -!- DOMAIN: Binds three molecules of c-di-AMP, each in a pocket located
CC       between two subunits. c-di-AMP binding is accompanied by conformational
CC       changes of both the fold and the position of the B-loop.
CC       {ECO:0000269|PubMed:25433025}.
CC   -!- DISRUPTION PHENOTYPE: Not essential. {ECO:0000269|PubMed:25433025}.
DR   EMBL; D26185; BAA05265.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11805.1; -; Genomic_DNA.
DR   PIR; S66059; S66059.
DR   RefSeq; NP_387910.1; NC_000964.3.
DR   RefSeq; WP_003242755.1; NZ_JNCM01000028.1.
DR   PDB; 4RLE; X-ray; 1.30 A; A=1-109.
DR   PDBsum; 4RLE; -.
DR   SMR; P37538; -.
DR   STRING; 224308.BSU00290; -.
DR   jPOST; P37538; -.
DR   PaxDb; P37538; -.
DR   PRIDE; P37538; -.
DR   EnsemblBacteria; CAB11805; CAB11805; BSU00290.
DR   GeneID; 938610; -.
DR   KEGG; bsu:BSU00290; -.
DR   PATRIC; fig|224308.179.peg.29; -.
DR   eggNOG; ENOG4105X0R; Bacteria.
DR   eggNOG; COG3870; LUCA.
DR   HOGENOM; HOG000083378; -.
DR   InParanoid; P37538; -.
DR   OMA; TFMIGIE; -.
DR   PhylomeDB; P37538; -.
DR   BioCyc; BSUB:BSU00290-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   Gene3D; 3.30.70.120; -; 1.
DR   InterPro; IPR010375; CdAMP_rec.
DR   InterPro; IPR011322; N-reg_PII-like_a/b.
DR   InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR   PANTHER; PTHR38456; PTHR38456; 1.
DR   Pfam; PF06153; CdAMP_rec; 1.
DR   SUPFAM; SSF54913; SSF54913; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37538.
DR   SWISS-2DPAGE; P37538.
KW   3D-structure; Reference proteome.
FT   CHAIN           1..109
FT                   /note="Cyclic di-AMP receptor A"
FT                   /id="PRO_0000049435"
FT   REGION          25..28
FT                   /note="c-di-AMP binding"
FT                   /evidence="ECO:0000269|PubMed:25433025"
FT   REGION          35..37
FT                   /note="c-di-AMP binding"
FT                   /evidence="ECO:0000269|PubMed:25433025"
FT   REGION          92..94
FT                   /note="c-di-AMP binding"
FT                   /evidence="ECO:0000269|PubMed:25433025"
FT   BINDING         21
FT                   /note="c-di-AMP; via carbonyl oxygen"
FT                   /evidence="ECO:0000269|PubMed:25433025"
FT   BINDING         41
FT                   /note="c-di-AMP"
FT                   /evidence="ECO:0000269|PubMed:25433025"
FT   BINDING         47
FT                   /note="c-di-AMP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000269|PubMed:25433025"
FT   STRAND          1..8
FT                   /evidence="ECO:0000244|PDB:4RLE"
FT   HELIX           10..22
FT                   /evidence="ECO:0000244|PDB:4RLE"
FT   STRAND          28..33
FT                   /evidence="ECO:0000244|PDB:4RLE"
FT   TURN            35..37
FT                   /evidence="ECO:0000244|PDB:4RLE"
FT   STRAND          39..49
FT                   /evidence="ECO:0000244|PDB:4RLE"
FT   HELIX           50..52
FT                   /evidence="ECO:0000244|PDB:4RLE"
FT   HELIX           53..63
FT                   /evidence="ECO:0000244|PDB:4RLE"
FT   STRAND          67..70
FT                   /evidence="ECO:0000244|PDB:4RLE"
FT   TURN            76..83
FT                   /evidence="ECO:0000244|PDB:4RLE"
FT   STRAND          90..93
FT                   /evidence="ECO:0000244|PDB:4RLE"
FT   STRAND          95..102
FT                   /evidence="ECO:0000244|PDB:4RLE"
SQ   SEQUENCE   109 AA;  11967 MW;  15827F78355C0981 CRC64;
     MKLIVAVVQD QDSNRLLKTL TDHNFRVTKL ATTGGFLKSG NTTFMIGVED IRVNKALSLI
     KENGQKRDQM IAPVSPMGGN ADSYVPYPVE VEVGGATVFV LPVDEFHQF
//

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