CDAR_BACSU
ID CDAR_BACSU Reviewed; 483 AA.
AC O34659; O87088;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=CdaA regulatory protein CdaR {ECO:0000305};
DE AltName: Full=YbbR-like domain-containing protein YbbR;
DE AltName: Full=c-di-AMP synthase A regulator {ECO:0000303|PubMed:23192352};
GN Name=cdaR {ECO:0000303|PubMed:23192352}; Synonyms=ybbR;
GN OrderedLocusNames=BSU01760;
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;
RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT Bacillus subtilis chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, INTERACTION WITH CDAA, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
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 [4]
RP INTERACTION WITH CDAA.
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: Upon coexpression in E.coli stimulates the diadenylate
CC cyclase activity of CdaA about 20-fold (PubMed:23192352). In B.subtilis
CC c-di-AMP is a second messenger that mediates growth, DNA repair and
CC cell wall homeostasis; it is toxic when present in excess
CC (PubMed:26240071). {ECO:0000269|PubMed:23192352,
CC ECO:0000269|PubMed:26240071}.
CC -!- SUBUNIT: Interacts with CdaA (PubMed:23192352, PubMed:26240071).
CC {ECO:0000269|PubMed:23192352, ECO:0000269|PubMed:26240071}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Constitutively expressed, part of the cdaA-cdaR-glmM-glmS
CC operon (PubMed:23192352). {ECO:0000269|PubMed:23192352}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:26240071}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA33068.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB006424; BAA33068.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB11952.2; -; Genomic_DNA.
DR RefSeq; NP_388057.2; NC_000964.3.
DR RefSeq; WP_003234947.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; O34659; -.
DR SMR; O34659; -.
DR STRING; 224308.BSU01760; -.
DR PaxDb; O34659; -.
DR DNASU; 938867; -.
DR EnsemblBacteria; CAB11952; CAB11952; BSU_01760.
DR GeneID; 938867; -.
DR KEGG; bsu:BSU01760; -.
DR PATRIC; fig|224308.179.peg.182; -.
DR eggNOG; COG4856; Bacteria.
DR InParanoid; O34659; -.
DR OMA; NNRWAVK; -.
DR PhylomeDB; O34659; -.
DR BioCyc; BSUB:BSU01760-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IDA:UniProtKB.
DR InterPro; IPR012505; YbbR.
DR Pfam; PF07949; YbbR; 4.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..483
FT /note="CdaA regulatory protein CdaR"
FT /id="PRO_0000384386"
FT TRANSMEM 9..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 55..135
FT /note="YbbR-like 1"
FT DOMAIN 143..228
FT /note="YbbR-like 2"
FT DOMAIN 237..316
FT /note="YbbR-like 3"
FT DOMAIN 329..394
FT /note="YbbR-like 4"
FT REGION 410..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 186
FT /note="V -> H (in Ref. 1; BAA33068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 52907 MW; C591A9A3106D7BC2 CRC64;
MDKFLNNRWA VKIIALLFAL LLYVAVNSNQ APTPKKPGES FFPTSTTDEA TLTDIPVKAY
YDDENYVVTG VPQTVNVTIK GSTSAVKKAR QTKNFEIYAD MEHLKTGTHK VELKAKNVSD
GLTISINPSV TTVTIQERTT KSFPVEVEYY NKSKMKKGYS PEQPIVSPKN VQITGSKNVI
DNISLVKASV NLENADETIE KEAKVTVYDK DGNALPVDVE PSVIKITVPV TSPSKKVPFK
IERTGSLPDG VSIANIESSP SEVTVYGSQD VLDSLEFIDG VSLDLSKINK DSDIEADIPL
PDGVKKISPS KVTLHIEVDS EADQKFENVP IKTVGLSSSQ NIEFLDPESQ AIDVTAKGSP
TNINKLKKSD IELYVNVSDL EDGEHSVKLE VNGPQNVTWS LGRKNAKIKL TSKKSNTSTN
DNSSNTSGNQ DTDKQTNDQK NNQQEDTKNT DKNNNDQNQD GNKDQNQDQD EDESTANSQS
SSE
