P0A9G8 · MODE_ECOLI
- ProteinDNA-binding transcriptional dual regulator ModE
- GenemodE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids262 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as an intracellular molybdate sensor. The ModE-Mo complex acts as a repressor of the modABC operon, which is involved in the transport of molybdate (PubMed:8550508).
Binds modA promoter DNA in the absence of molybdate, however molybdate binding confers increased DNA affinity (PubMed:9044285, PubMed:9210473).
Binds the promoter of moaA activating its transcription; binding is not enhanced by molybdate (PubMed:9044285).
The protein dimer binds the consensus palindrome sequence 5'-TATAT-N7-TAYAT-3' and a variant 5'-TGTGT-N7-TGYGT-3' (PubMed:16205910, PubMed:9044285, PubMed:9210473).
Acts as a regulator of the expression of 67 genes, many of which encode molybdoenzymes, acts both directly and indirectly (PubMed:10206709, PubMed:16205910, PubMed:9466267).
ModE also binds tungstate (PubMed:11259434, PubMed:9210473).
Binds modA promoter DNA in the absence of molybdate, however molybdate binding confers increased DNA affinity (PubMed:9044285, PubMed:9210473).
Binds the promoter of moaA activating its transcription; binding is not enhanced by molybdate (PubMed:9044285).
The protein dimer binds the consensus palindrome sequence 5'-TATAT-N7-TAYAT-3' and a variant 5'-TGTGT-N7-TGYGT-3' (PubMed:16205910, PubMed:9044285, PubMed:9210473).
Acts as a regulator of the expression of 67 genes, many of which encode molybdoenzymes, acts both directly and indirectly (PubMed:10206709, PubMed:16205910, PubMed:9466267).
ModE also binds tungstate (PubMed:11259434, PubMed:9210473).
Activity regulation
The ModE dimer binds two molecules of molybdate (MoO42-) with a Kd of 0.8 uM, which results in major changes in the conformation of the DNA-binding domain and confers high-affinity DNA-binding to the transcription factor (PubMed:11259434, PubMed:12581638, PubMed:9044285, PubMed:9210473).
Additionally molybdate binding moves the 2 Mop domains closer together, trapping the ligand between them (PubMed:12581638).
Can also bind tungstate (PubMed:11259434, PubMed:9210473).
Molybdate is bound at the dimer interface using residues from each monomer (PubMed:11259434, PubMed:12581638).
Additionally molybdate binding moves the 2 Mop domains closer together, trapping the ligand between them (PubMed:12581638).
Can also bind tungstate (PubMed:11259434, PubMed:9210473).
Molybdate is bound at the dimer interface using residues from each monomer (PubMed:11259434, PubMed:12581638).
Features
Showing features for dna binding, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
DNA binding | 33-79 | H-T-H motif | |||
Binding site | 126 | molybdate (UniProtKB | ChEBI) | |||
Binding site | 128 | molybdate (UniProtKB | ChEBI) | |||
Binding site | 163 | molybdate (UniProtKB | ChEBI) | |||
Binding site | 166 | molybdate (UniProtKB | ChEBI) | |||
Binding site | 183 | molybdate (UniProtKB | ChEBI) | |||
Binding site | 184 | molybdate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | ModE complex | |
Molecular Function | cis-regulatory region sequence-specific DNA binding | |
Molecular Function | molybdenum ion binding | |
Biological Process | molybdate ion transport | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of DNA-templated transcription initiation | |
Biological Process | positive regulation of DNA-templated transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA-binding transcriptional dual regulator ModE
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0A9G8
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Loss of repression of the modABC operon (PubMed:8564363, PubMed:8931336).
Not essential for molybdopterin cofactor synthesis (PubMed:8931336).
Increased dmsA expression under aerobic conditions and reduced expression under anaerobic conditions (PubMed:9466267).
Decreased expression of hyc and narG (PubMed:10206709).
Not essential for molybdopterin cofactor synthesis (PubMed:8931336).
Increased dmsA expression under aerobic conditions and reduced expression under anaerobic conditions (PubMed:9466267).
Decreased expression of hyc and narG (PubMed:10206709).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 76 | Partial loss of repression by ModE. | |||
Mutagenesis | 125 | Transcription repression by ModE even in the absence of molybdate. | |||
Mutagenesis | 133 | Transcription repression by ModE even in the absence of molybdate. | |||
Mutagenesis | 216-262 | Transcription repression by ModE even in the absence of molybdate. | |||
Interaction
Subunit
Homodimer.
Complex viewer
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-121 | I | |||
Domain | 124-191 | Mop 1 | |||
Region | 125-133 | Required for dimer formation and molybdate binding | |||
Domain | 196-260 | Mop 2 | |||
Domain
Deletion of the C-terminus (from residues 122 on) results in constitutive repression of modA (PubMed:8931336).
Contains two major domains: the N-terminal domain I forms a winged helix-turn-helix motif and interacts with DNA (Probable). The C-terminal domain II is the olybdate-binding component and contains a tandem repeat of the Mop domain, each of which forms a beta-barrel (Probable) (PubMed:12581638).
The N-terminal domain plays a major role in the dimerization of the protein whereas the C-terminal domain contributes to the stability of the complex (Probable)
Contains two major domains: the N-terminal domain I forms a winged helix-turn-helix motif and interacts with DNA (Probable). The C-terminal domain II is the olybdate-binding component and contains a tandem repeat of the Mop domain, each of which forms a beta-barrel (Probable) (PubMed:12581638).
The N-terminal domain plays a major role in the dimerization of the protein whereas the C-terminal domain contributes to the stability of the complex (Probable)
Sequence similarities
Belongs to the ModE family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length262
- Mass (Da)28,281
- Last updated2005-07-19 v1
- MD5 Checksum0B06EAB3EFDE23CE54D4F3D54D8C0318
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U07867 EMBL· GenBank· DDBJ | AAB06892.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U27192 EMBL· GenBank· DDBJ | AAB60175.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U34275 EMBL· GenBank· DDBJ | AAA77051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73848.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA35425.1 EMBL· GenBank· DDBJ | Genomic DNA |