GBSR_BACSU
ID GBSR_BACSU Reviewed; 180 AA.
AC P71015;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=HTH-type transcriptional repressor GbsR;
DE AltName: Full=Glycine betaine synthesis regulator;
GN Name=gbsR; Synonyms=yuaC; OrderedLocusNames=BSU31070;
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 / JH642;
RX PubMed=8752328; DOI=10.1128/jb.178.17.5121-5129.1996;
RA Boch J., Kempf B., Schmid R., Bremer E.;
RT "Synthesis of the osmoprotectant glycine betaine in Bacillus subtilis:
RT characterization of the gbsAB genes.";
RL J. Bacteriol. 178:5121-5129(1996).
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, ACTIVITY REGULATION, AND GENE NAME.
RC STRAIN=168 / JH642;
RX PubMed=22408163; DOI=10.1128/jb.06642-11;
RA Nau-Wagner G., Opper D., Rolbetzki A., Boch J., Kempf B., Hoffmann T.,
RA Bremer E.;
RT "Genetic control of osmoadaptive glycine betaine synthesis in Bacillus
RT subtilis through the choline-sensing and glycine betaine-responsive GbsR
RT repressor.";
RL J. Bacteriol. 194:2703-2714(2012).
CC -!- FUNCTION: Negatively regulates the expression of the gbsAB and opuB
CC operons. Required to control expression of these genes in response to
CC choline availability. Also required to down-regulate glycine betaine
CC production once cellular adjustment to high osmolarity has been
CC achieved. {ECO:0000269|PubMed:22408163}.
CC -!- ACTIVITY REGULATION: Intracellular choline sensor. Binding to choline
CC induces conformational changes and relieves the repressing effects of
CC GbsR on expression. {ECO:0000269|PubMed:22408163}.
CC -!- SIMILARITY: Belongs to the GbsR family. {ECO:0000305}.
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DR EMBL; U47861; AAC44366.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15085.1; -; Genomic_DNA.
DR PIR; E70005; E70005.
DR RefSeq; NP_390985.1; NC_000964.3.
DR RefSeq; WP_003244320.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P71015; -.
DR SMR; P71015; -.
DR STRING; 224308.BSU31070; -.
DR PaxDb; P71015; -.
DR EnsemblBacteria; CAB15085; CAB15085; BSU_31070.
DR GeneID; 938843; -.
DR KEGG; bsu:BSU31070; -.
DR PATRIC; fig|224308.179.peg.3367; -.
DR eggNOG; COG1510; Bacteria.
DR InParanoid; P71015; -.
DR OMA; MYMRDEM; -.
DR PhylomeDB; P71015; -.
DR BioCyc; BSUB:BSU31070-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR026282; MJ1563.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PIRSF; PIRSF006707; MJ1563; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 3: Inferred from homology;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..180
FT /note="HTH-type transcriptional repressor GbsR"
FT /id="PRO_0000049912"
FT DNA_BIND 49..73
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
SQ SEQUENCE 180 AA; 21070 MW; 64C91F3AF7E49E11 CRC64;
MDENPEFAAI EQARDLVIDS IAETMDLYGI TRSVGILYGT MYMRDEMTLD EMREELQMSK
PSMSTGVKKL QDLNVVKKTF HRGIRKHTFV AEKDFFKFFT NFFPPKWERE VQVNVTAIEE
AQADLQKVLC KEDLDEDIKN EALQLYDQLE SSKAYYDWLK RLAESVQTGE IFKFIPVETK