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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)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

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)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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi94 – 104Combined sources11
Beta strandi108 – 115Combined sources8
Turni117 – 119Combined sources3
Helixi122 – 138Combined sources17
Beta strandi141 – 147Combined sources7
Helixi151 – 159Combined sources9
Beta strandi168 – 177Combined sources10
Beta strandi179 – 181Combined sources3
Helixi182 – 184Combined sources3
Helixi185 – 197Combined sources13
Helixi212 – 219Combined sources8
Helixi222 – 232Combined sources11
Beta strandi235 – 239Combined sources5
Helixi244 – 250Combined sources7
Helixi255 – 263Combined sources9
Beta strandi266 – 270Combined sources5
Beta strandi273 – 276Combined sources4
Beta strandi281 – 284Combined sources4
Beta strandi286 – 289Combined sources4
Helixi292 – 297Combined sources6
Beta strandi299 – 304Combined sources6
Helixi308 – 310Combined sources3
Helixi311 – 317Combined sources7
Beta strandi324 – 329Combined sources6
Helixi330 – 337Combined sources8

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...

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.
OMAiANTICAH.
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
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.
PATRICi18978790. VBIBacSub10457_3558.

Phylogenomic databases

eggNOGiCOG2390. LUCA.
HOGENOMiHOG000071790.
KOiK05311.
OMAiANTICAH.
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...

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: November 2, 2016
This is version 109 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.