CGGR_BACSU
ID CGGR_BACSU Reviewed; 340 AA.
AC O32253;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Central glycolytic genes regulator;
GN Name=cggR; Synonyms=yvbQ; OrderedLocusNames=BSU33950;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP FUNCTION, AND GENE NAME.
RX PubMed=10799476; DOI=10.1074/jbc.275.19.14031;
RA Fillinger S., Boschi-Muller S., Azza S., Dervyn E., Branlant G.,
RA Aymerich S.;
RT "Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological
RT roles in a nonphotosynthetic bacterium.";
RL J. Biol. Chem. 275:14031-14037(2000).
RN [3]
RP FUNCTION, DNA-BINDING, AND ACTIVITY REGULATION.
RC STRAIN=168;
RX PubMed=12622823; DOI=10.1046/j.1365-2958.2003.03404.x;
RA Doan T., Aymerich S.;
RT "Regulation of the central glycolytic genes in Bacillus subtilis: binding
RT of the repressor CggR to its single DNA target sequence is modulated by
RT fructose-1,6-bisphosphate.";
RL Mol. Microbiol. 47:1709-1721(2003).
RN [4]
RP ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=18052209; DOI=10.1021/bi701805e;
RA Zorrilla S., Chaix D., Ortega A., Alfonso C., Doan T., Margeat E.,
RA Rivas G., Aymerich S., Declerck N., Royer C.A.;
RT "Fructose-1,6-bisphosphate acts both as an inducer and as a structural
RT cofactor of the central glycolytic genes repressor (CggR).";
RL Biochemistry 46:14996-15008(2007).
RN [5]
RP DNA-BINDING, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=17293407; DOI=10.1529/biophysj.106.095109;
RA Zorrilla S., Doan T., Alfonso C., Margeat E., Ortega A., Rivas G.,
RA Aymerich S., Royer C.A., Declerck N.;
RT "Inducer-modulated cooperative binding of the tetrameric CggR repressor to
RT operator DNA.";
RL Biophys. J. 92:3215-3227(2007).
RN [6]
RP ACTIVITY REGULATION, SUBUNIT, AND DOMAIN.
RX PubMed=20361740; DOI=10.1021/ac902784n;
RA Atmanene C., Chaix D., Bessin Y., Declerck N., Van Dorsselaer A.,
RA Sanglier-Cianferani S.;
RT "Combination of noncovalent mass spectrometry and traveling wave ion
RT mobility spectrometry reveals sugar-induced conformational changes of
RT central glycolytic genes repressor/DNA complex.";
RL Anal. Chem. 82:3597-3605(2010).
RN [7]
RP FUNCTION, DNA-BINDING, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=20462860; DOI=10.1093/nar/gkq334;
RA Chaix D., Ferguson M.L., Atmanene C., Van Dorsselaer A.,
RA Sanglier-Cianferani S., Royer C.A., Declerck N.;
RT "Physical basis of the inducer-dependent cooperativity of the Central
RT glycolytic genes Repressor/DNA complex.";
RL Nucleic Acids Res. 38:5944-5957(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 89-340 OF APOPROTEIN AND IN
RP COMPLEXES WITH BETA-FRUCTOSE-1,6-BISPHOSPHATE;
RP 1,3-DIHYDROXYACETONEPHOSPHATE; FRUCTOSE-6-PHOSPHATE AND BETA-D-GLUCOSE
RP 6-PHOSPHATE, ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=18554327; DOI=10.1111/j.1365-2958.2008.06318.x;
RA Rezacova P., Kozisek M., Moy S.F., Sieglova I., Joachimiak A., Machius M.,
RA Otwinowski Z.;
RT "Crystal structures of the effector-binding domain of repressor central
RT glycolytic gene regulator from Bacillus subtilis reveal ligand-induced
RT structural changes upon binding of several glycolytic intermediates.";
RL Mol. Microbiol. 69:895-910(2008).
CC -!- FUNCTION: In the absence of glucose, represses the transcription of the
CC gapA operon, which encodes five key glycolytic enzymes. Binds
CC specifically to the cggR-gapA promoter region and blocks the
CC progression of the RNA polymerase, leading to the arrest of the
CC transcription. {ECO:0000269|PubMed:10799476,
CC ECO:0000269|PubMed:12622823, ECO:0000269|PubMed:20462860}.
CC -!- ACTIVITY REGULATION: Stability and function are regulated by the
CC effector molecule fructose-1,6-bisphosphate (FBP). In the presence of
CC glucose, binding of FBP to the low-affinity sugar-binding site of CggR
CC disrupts dimer/dimer bridging interactions and triggers a tetramer to
CC dimer transition, which leaves two physically independent dimers on the
CC target DNA and allows transcription of the downstream coding sequences
CC by the RNA polymerase. In addition, FBP and several other
CC phosphorylated compounds can bind to a high-affinity binding-site and
CC protect CggR against aggregation and proteolysis.
CC {ECO:0000269|PubMed:12622823, ECO:0000269|PubMed:17293407,
CC ECO:0000269|PubMed:18052209, ECO:0000269|PubMed:18554327,
CC ECO:0000269|PubMed:20361740, ECO:0000269|PubMed:20462860}.
CC -!- SUBUNIT: Homotetramer. Binds primarily as a dimer to each half-site of
CC the full-length operator, with much higher affinity for the right site.
CC Then, both dimers interact, bridging the two-half sites of the operator
CC region. {ECO:0000269|PubMed:17293407, ECO:0000269|PubMed:20361740,
CC ECO:0000269|PubMed:20462860}.
CC -!- DOMAIN: Contains an N-terminal DNA-binding domain and a large C-
CC terminal effector-binding domain. Contains two distinct sugar-binding
CC sites with different affinities. {ECO:0000269|PubMed:18052209,
CC ECO:0000269|PubMed:18554327, ECO:0000269|PubMed:20361740}.
CC -!- SIMILARITY: Belongs to the SorC transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB15400.1; -; Genomic_DNA.
DR PIR; C70030; C70030.
DR RefSeq; NP_391275.1; NC_000964.3.
DR RefSeq; WP_009968188.1; NZ_JNCM01000033.1.
DR PDB; 2OKG; X-ray; 1.65 A; A/B=89-340.
DR PDB; 3BXE; X-ray; 1.80 A; A/B=89-340.
DR PDB; 3BXF; X-ray; 1.70 A; A/B=89-340.
DR PDB; 3BXG; X-ray; 1.80 A; A/B=89-340.
DR PDB; 3BXH; X-ray; 1.85 A; A/B=89-340.
DR PDB; 7OYK; X-ray; 2.10 A; AAA/BBB/CCC/DDD=1-91.
DR PDBsum; 2OKG; -.
DR PDBsum; 3BXE; -.
DR PDBsum; 3BXF; -.
DR PDBsum; 3BXG; -.
DR PDBsum; 3BXH; -.
DR PDBsum; 7OYK; -.
DR AlphaFoldDB; O32253; -.
DR SMR; O32253; -.
DR STRING; 224308.BSU33950; -.
DR PaxDb; O32253; -.
DR PRIDE; O32253; -.
DR DNASU; 938570; -.
DR EnsemblBacteria; CAB15400; CAB15400; BSU_33950.
DR GeneID; 938570; -.
DR KEGG; bsu:BSU33950; -.
DR PATRIC; fig|224308.179.peg.3681; -.
DR eggNOG; COG2390; Bacteria.
DR OMA; SVAYYQD; -.
DR PhylomeDB; O32253; -.
DR BioCyc; BSUB:BSU33950-MON; -.
DR EvolutionaryTrace; O32253; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..340
FT /note="Central glycolytic genes regulator"
FT /id="PRO_0000062787"
FT DNA_BIND 37..56
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT BINDING 149..152
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="effector"
FT /evidence="ECO:0007744|PDB:3BXF"
FT BINDING 175
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="effector"
FT /evidence="ECO:0007744|PDB:3BXF"
FT BINDING 185
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="effector"
FT /evidence="ECO:0007744|PDB:3BXF"
FT BINDING 250..251
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="effector"
FT /evidence="ECO:0007744|PDB:3BXF"
FT BINDING 269
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="effector"
FT /evidence="ECO:0007744|PDB:3BXF"
FT BINDING 310
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="effector"
FT /evidence="ECO:0007744|PDB:3BXF"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:2OKG"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:2OKG"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:2OKG"
FT HELIX 122..138
FT /evidence="ECO:0007829|PDB:2OKG"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:2OKG"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:2OKG"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:2OKG"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3BXF"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3BXE"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:2OKG"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:2OKG"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:2OKG"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:2OKG"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:2OKG"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:2OKG"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:2OKG"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:2OKG"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:2OKG"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:2OKG"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:2OKG"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:2OKG"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:2OKG"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:2OKG"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:2OKG"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:2OKG"
SQ SEQUENCE 340 AA; 37382 MW; 18C885966DDB42DB CRC64;
MNQLIQAQKK LLPDLLLVMQ KRFEILQYIR LTEPIGRRSL SASLGISERV LRGEVQFLKE
QNLVDIKTNG MTLTEEGYEL LSVLEDTMKD VLGLTLLEKT LKERLNLKDA IIVSGDSDQS
PWVKKEMGRA AVACMKKRFS GKNIVAVTGG TTIEAVAEMM TPDSKNRELL FVPARGGLGE
DVKNQANTIC AHMAEKASGT YRLLFVPGQL SQGAYSSIIE EPSVKEVLNT IKSASMLVHG
IGEAKTMAQR RNTPLEDLKK IDDNDAVTEA FGYYFNADGE VVHKVHSVGM QLDDIDAIPD
IIAVAGGSSK AEAIEAYFKK PRNTVLVTDE GAAKKLLRDE
