GAMR_BACSU
ID GAMR_BACSU Reviewed; 235 AA.
AC O31459; Q7DL45;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=HTH-type transcriptional repressor GamR {ECO:0000305};
GN Name=gamR {ECO:0000303|PubMed:24673833}; Synonyms=ybgA;
GN OrderedLocusNames=BSU02370;
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, DNA-BINDING, AND ACTIVITY REGULATION.
RX PubMed=24673833; DOI=10.1111/mmi.12544;
RA Gaugue I., Oberto J., Plumbridge J.;
RT "Regulation of amino sugar utilization in Bacillus subtilis by the GntR
RT family regulators, NagR and GamR.";
RL Mol. Microbiol. 92:100-115(2014).
CC -!- FUNCTION: Transcriptional repressor of genes involved in glucosamine
CC transport and utilization. Represses the expression of the gamAP operon
CC by binding to the gamA-gamR intergenic region.
CC {ECO:0000269|PubMed:24673833}.
CC -!- ACTIVITY REGULATION: Binding to DNA is allosterically inhibited by the
CC effector glucosamine-6-phosphate (GlcN6P). N-acetylglucosamine-6-
CC phosphate (GlcNAc6P) and glucose-6-phosphate (Glc6P) have no effect.
CC {ECO:0000269|PubMed:24673833}.
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DR EMBL; AB006424; BAA33134.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12031.1; -; Genomic_DNA.
DR PIR; F69750; F69750.
DR RefSeq; NP_388119.1; NC_000964.3.
DR RefSeq; WP_003234841.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; O31459; -.
DR SMR; O31459; -.
DR STRING; 224308.BSU02370; -.
DR PaxDb; O31459; -.
DR PRIDE; O31459; -.
DR EnsemblBacteria; CAB12031; CAB12031; BSU_02370.
DR GeneID; 938422; -.
DR KEGG; bsu:BSU02370; -.
DR PATRIC; fig|224308.179.peg.243; -.
DR eggNOG; COG2188; Bacteria.
DR InParanoid; O31459; -.
DR OMA; SRYSFEF; -.
DR PhylomeDB; O31459; -.
DR BioCyc; BSUB:BSU02370-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.1410.10; -; 1.
DR InterPro; IPR028978; Chorismate_lyase_/UTRA_dom_sf.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR011663; UTRA.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00392; GntR; 1.
DR Pfam; PF07702; UTRA; 1.
DR PRINTS; PR00035; HTHGNTR.
DR SMART; SM00345; HTH_GNTR; 1.
DR SMART; SM00866; UTRA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF64288; SSF64288; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..235
FT /note="HTH-type transcriptional repressor GamR"
FT /id="PRO_0000360573"
FT DOMAIN 2..70
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT DNA_BIND 30..49
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
SQ SEQUENCE 235 AA; 26603 MW; E7AFB934DD2FE570 CRC64;
MTALYSVIKF KIIELIKSGK YQANDQLPTE SEFCEQYDVS RTTVRLALQQ LELEGYIKRI
QGKGTFVSAA KIQTPIPHKI TSFAEQMRGL RSESKVLELV VIPADHSIAE LLKMKENEPV
NKLVRVRYAE GEPLQYHTSY IPWKAAPGLA QEECTGSLFE LLRTKYNIEI SRGTESIEPI
LTDETISGHL LTNVGAPAFL SESLTYDKNE EVVEYAQIIT RGDRTKFTVE QSYHS
