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Protein

Central glycolytic genes regulator

Gene

cggR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

In the absence of glucose, represses the transcription of the gapA operon, which encodes five key glycolytic enzymes. Binds specifically to the cggR-gapA promoter region and blocks the progression of the RNA polymerase, leading to the arrest of the transcription.3 Publications

Enzyme regulationi

Stability and function are regulated by the effector molecule fructose-1,6-bisphosphate (FBP). In the presence of glucose, binding of FBP to the low-affinity sugar-binding site of CggR disrupts dimer/dimer bridging interactions and triggers a tetramer to dimer transition, which leaves two physically independent dimers on the target DNA and allows transcription of the downstream coding sequences by the RNA polymerase. In addition, FBP and several other phosphorylated compounds can bind to a high-affinity binding-site and protect CggR against aggregation and proteolysis.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei175 – 1751Effector
Binding sitei185 – 1851Effector
Binding sitei269 – 2691Effector
Binding sitei310 – 3101Effector

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi37 – 5620H-T-H motifSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU33950-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Central glycolytic genes regulator
Gene namesi
Name:cggR
Synonyms:yvbQ
Ordered Locus Names:BSU33950
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Central glycolytic genes regulatorPRO_0000062787Add
BLAST

Proteomic databases

PaxDbiO32253.

Interactioni

Subunit structurei

Homotetramer. Binds primarily as a dimer to each half-site of the full-length operator, with much higher affinity for the right site. Then, both dimers interact, bridging the two-half sites of the operator region.3 Publications

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018416.

Structurei

Secondary structure

1
340
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi94 – 10411Combined sources
Beta strandi108 – 1158Combined sources
Turni117 – 1193Combined sources
Helixi122 – 13817Combined sources
Beta strandi141 – 1477Combined sources
Helixi151 – 1599Combined sources
Beta strandi168 – 17710Combined sources
Beta strandi179 – 1813Combined sources
Helixi182 – 1843Combined sources
Helixi185 – 19713Combined sources
Helixi212 – 2198Combined sources
Helixi222 – 23211Combined sources
Beta strandi235 – 2395Combined sources
Helixi244 – 2507Combined sources
Helixi255 – 2639Combined sources
Beta strandi266 – 2705Combined sources
Beta strandi273 – 2764Combined sources
Beta strandi281 – 2844Combined sources
Beta strandi286 – 2894Combined sources
Helixi292 – 2976Combined sources
Beta strandi299 – 3046Combined sources
Helixi308 – 3103Combined sources
Helixi311 – 3177Combined sources
Beta strandi324 – 3296Combined sources
Helixi330 – 3378Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OKGX-ray1.65A/B89-340[»]
3BXEX-ray1.80A/B89-340[»]
3BXFX-ray1.70A/B89-340[»]
3BXGX-ray1.80A/B89-340[»]
3BXHX-ray1.85A/B89-340[»]
ProteinModelPortaliO32253.
SMRiO32253. Positions 21-338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO32253.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 1524Effector binding
Regioni250 – 2512Effector binding

Domaini

Contains an N-terminal DNA-binding domain and a large C-terminal effector-binding domain. Contains two distinct sugar-binding sites with different affinities.3 Publications

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2390. LUCA.
HOGENOMiHOG000071790.
KOiK05311.
OMAiANTICAH.
OrthoDBiEOG6SR93K.
PhylomeDBiO32253.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR007324. Sugar-bd_dom_put.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF04198. Sugar-bind. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

O32253-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQLIQAQKK LLPDLLLVMQ KRFEILQYIR LTEPIGRRSL SASLGISERV
60 70 80 90 100
LRGEVQFLKE QNLVDIKTNG MTLTEEGYEL LSVLEDTMKD VLGLTLLEKT
110 120 130 140 150
LKERLNLKDA IIVSGDSDQS PWVKKEMGRA AVACMKKRFS GKNIVAVTGG
160 170 180 190 200
TTIEAVAEMM TPDSKNRELL FVPARGGLGE DVKNQANTIC AHMAEKASGT
210 220 230 240 250
YRLLFVPGQL SQGAYSSIIE EPSVKEVLNT IKSASMLVHG IGEAKTMAQR
260 270 280 290 300
RNTPLEDLKK IDDNDAVTEA FGYYFNADGE VVHKVHSVGM QLDDIDAIPD
310 320 330 340
IIAVAGGSSK AEAIEAYFKK PRNTVLVTDE GAAKKLLRDE
Length:340
Mass (Da):37,382
Last modified:January 1, 1998 - v1
Checksum:i18C885966DDB42DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15400.1.
PIRiC70030.
RefSeqiNP_391275.1. NC_000964.3.
WP_009968188.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15400; CAB15400; BSU33950.
GeneIDi938570.
KEGGibsu:BSU33950.
PATRICi18978790. VBIBacSub10457_3558.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15400.1.
PIRiC70030.
RefSeqiNP_391275.1. NC_000964.3.
WP_009968188.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OKGX-ray1.65A/B89-340[»]
3BXEX-ray1.80A/B89-340[»]
3BXFX-ray1.70A/B89-340[»]
3BXGX-ray1.80A/B89-340[»]
3BXHX-ray1.85A/B89-340[»]
ProteinModelPortaliO32253.
SMRiO32253. Positions 21-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018416.

Proteomic databases

PaxDbiO32253.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15400; CAB15400; BSU33950.
GeneIDi938570.
KEGGibsu:BSU33950.
PATRICi18978790. VBIBacSub10457_3558.

Phylogenomic databases

eggNOGiCOG2390. LUCA.
HOGENOMiHOG000071790.
KOiK05311.
OMAiANTICAH.
OrthoDBiEOG6SR93K.
PhylomeDBiO32253.

Enzyme and pathway databases

BioCyciBSUB:BSU33950-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO32253.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR007324. Sugar-bd_dom_put.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF04198. Sugar-bind. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium."
    Fillinger S., Boschi-Muller S., Azza S., Dervyn E., Branlant G., Aymerich S.
    J. Biol. Chem. 275:14031-14037(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GENE NAME.
  3. "Regulation of the central glycolytic genes in Bacillus subtilis: binding of the repressor CggR to its single DNA target sequence is modulated by fructose-1,6-bisphosphate."
    Doan T., Aymerich S.
    Mol. Microbiol. 47:1709-1721(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, ENZYME REGULATION.
    Strain: 168.
  4. "Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR)."
    Zorrilla S., Chaix D., Ortega A., Alfonso C., Doan T., Margeat E., Rivas G., Aymerich S., Declerck N., Royer C.A.
    Biochemistry 46:14996-15008(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, DOMAIN.
  5. "Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA."
    Zorrilla S., Doan T., Alfonso C., Margeat E., Ortega A., Rivas G., Aymerich S., Royer C.A., Declerck N.
    Biophys. J. 92:3215-3227(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, ENZYME REGULATION, SUBUNIT.
  6. "Combination of noncovalent mass spectrometry and traveling wave ion mobility spectrometry reveals sugar-induced conformational changes of central glycolytic genes repressor/DNA complex."
    Atmanene C., Chaix D., Bessin Y., Declerck N., Van Dorsselaer A., Sanglier-Cianferani S.
    Anal. Chem. 82:3597-3605(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBUNIT, DOMAIN.
  7. "Physical basis of the inducer-dependent cooperativity of the Central glycolytic genes Repressor/DNA complex."
    Chaix D., Ferguson M.L., Atmanene C., Van Dorsselaer A., Sanglier-Cianferani S., Royer C.A., Declerck N.
    Nucleic Acids Res. 38:5944-5957(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, ENZYME REGULATION, SUBUNIT.
  8. "Crystal structures of the effector-binding domain of repressor central glycolytic gene regulator from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates."
    Rezacova P., Kozisek M., Moy S.F., Sieglova I., Joachimiak A., Machius M., Otwinowski Z.
    Mol. Microbiol. 69:895-910(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 89-340 OF APOPROTEIN AND IN COMPLEXES WITH BETA-FRUCTOSE-1,6-BISPHOSPHATE; 1,3-DIHYDROXYACETONEPHOSPHATE; FRUCTOSE-6-PHOSPHATE AND BETA-D-GLUCOSE 6-PHOSPHATE, ENZYME REGULATION, DOMAIN.

Entry informationi

Entry nameiCGGR_BACSU
AccessioniPrimary (citable) accession number: O32253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.