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Protein

Central glycolytic genes regulator

Gene

cggR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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

Activity 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)DescriptionActionsGraphical viewLength
Binding sitei175Effector1
Binding sitei185Effector1
Binding sitei269Effector1
Binding sitei310Effector1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi37 – 56H-T-H motifSequence analysisAdd BLAST20

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Repressor
Biological processTranscription, Transcription regulation

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000627871 – 340Central glycolytic genes regulatorAdd BLAST340

Proteomic databases

PaxDbiO32253
PRIDEiO32253

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

1340
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO32253
SMRiO32253
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO32253

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni149 – 152Effector binding4
Regioni250 – 251Effector binding2

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
OMAiSSWSQTI
PhylomeDBiO32253

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR037171 NagB/RpiA_transferase-like
IPR007324 Sugar-bd_dom_put
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF04198 Sugar-bind, 1 hit
SUPFAMiSSF100950 SSF100950, 1 hit
SSF46785 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
PATRICifig|224308.179.peg.3681

Similar proteinsi

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
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018416

Proteomic databases

PaxDbiO32253
PRIDEiO32253

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15400; CAB15400; BSU33950
GeneIDi938570
KEGGibsu:BSU33950
PATRICifig|224308.179.peg.3681

Phylogenomic databases

eggNOGiCOG2390 LUCA
HOGENOMiHOG000071790
KOiK05311
OMAiSSWSQTI
PhylomeDBiO32253

Enzyme and pathway databases

BioCyciBSUB:BSU33950-MONOMER

Miscellaneous databases

EvolutionaryTraceiO32253

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR037171 NagB/RpiA_transferase-like
IPR007324 Sugar-bd_dom_put
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF04198 Sugar-bind, 1 hit
SUPFAMiSSF100950 SSF100950, 1 hit
SSF46785 SSF46785, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCGGR_BACSU
AccessioniPrimary (citable) accession number: O32253
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: September 12, 2018
This is version 113 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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