ID   CGGR_PRIM3              Reviewed;         342 AA.
AC   P35168; D5DNB2;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Central glycolytic genes regulator;
GN   Name=cggR; OrderedLocusNames=BMD_5039;
OS   Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=592022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1452037; DOI=10.1016/0378-1119(92)90031-j;
RA   Schlaepfer B.S., Zuber H.;
RT   "Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate
RT   dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase (gap
RT   operon) from mesophilic Bacillus megaterium: comparison with corresponding
RT   sequences from thermophilic Bacillus stearothermophilus.";
RL   Gene 122:53-62(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 319 / IMG 1521;
RX   PubMed=21705586; DOI=10.1128/jb.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
CC   -!- FUNCTION: In the absence of glucose, represses the transcription of the
CC       gapA operon, which encodes five key glycolytic enzymes. {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SorC transcriptional regulatory family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M87647; AAA73201.1; -; Genomic_DNA.
DR   EMBL; CP001982; ADF41839.1; -; Genomic_DNA.
DR   PIR; JQ1952; JQ1952.
DR   RefSeq; WP_013085386.1; NC_014103.1.
DR   AlphaFoldDB; P35168; -.
DR   SMR; P35168; -.
DR   EnsemblBacteria; ADF41839; ADF41839; BMD_5039.
DR   KEGG; bmd:BMD_5039; -.
DR   HOGENOM; CLU_054506_2_0_9; -.
DR   OMA; SVAYYQD; -.
DR   Proteomes; UP000002365; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR007324; Sugar-bd_dom_put.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF04198; Sugar-bind; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..342
FT                   /note="Central glycolytic genes regulator"
FT                   /id="PRO_0000062786"
FT   DNA_BIND        37..56
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   342 AA;  37726 MW;  95BC4FFA50CE06FD CRC64;
     MRSLIEVQRK LLPELLSVMQ KRYQILQYIR LMQPIGRRNL AVSLGLTERV LRSEVTFLKE
     QDLIDIYPSG MTLTNEGELL LAELEEVMKE VSGLRLLETT LKEAFSLSEV VVVSGDSDQS
     PWVKNEMGRA SVSCIKERLV GKKNTVAVTG GTTLAAVAEM MTPDLKHPDV LFVPARGGLG
     ENVQNQANTI CAKMAEKSMS HYRLLHVPDQ LSDEAYRSII GEPSIKDMLH LIKSAGMVVH
     GIGDAMTMAE RRKTPQADLE KVKNGHAVGE AFGYYFNHQG EVVHKVKTVG IQLDDLKNNK
     CVIAVAGGSS KAKAIKAFMQ QAHDSILITD EGAAKELVRD FN