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Protein

Transcriptional regulator ModE

Gene

modE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The ModE-Mo complex acts as a repressor of the modABC operon, involved in the transport of molybdate. Upon binding molybdate, the conformation of the protein changes, promoting dimerization of ModE-Mo. The protein dimer is then competent to bind a DNA region, upstream of the modABC operon, which contains an 8-base inverted repeat 5'-TAACGTTA-3' flanked by two CAT boxes. Acts also as an enhancer of the expression of genes coding for molybdoenzymes, both directly and indirectly. ModE also interacts with tungstate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi33 – 7947H-T-H motifAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Transport

Keywords - Ligandi

DNA-binding, Molybdenum

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-185.
ECOL316407:JW0744-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulator ModE
Gene namesi
Name:modE
Synonyms:modR
Ordered Locus Names:b0761, JW0744
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13227. modE.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi76 – 761A → V: Partial loss of repression by ModE. 1 Publication
Mutagenesisi125 – 1251T → I: Transcription repression by ModE even in the absence of molybdate. 1 Publication
Mutagenesisi133 – 1331G → D: Transcription repression by ModE even in the absence of molybdate. 1 Publication
Mutagenesisi216 – 26247Missing : Transcription repression by ModE even in the absence of molybdate. Add
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Transcriptional regulator ModEPRO_0000201125Add
BLAST

Proteomic databases

PaxDbiP0A9G8.
PRIDEiP0A9G8.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4259327. 4 interactions.
DIPiDIP-10238N.
IntActiP0A9G8. 1 interaction.
STRINGi511145.b0761.

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Beta strandi14 – 174Combined sources
Helixi19 – 3113Combined sources
Helixi34 – 418Combined sources
Helixi45 – 5915Combined sources
Beta strandi64 – 663Combined sources
Beta strandi76 – 783Combined sources
Helixi80 – 10526Combined sources
Helixi114 – 1218Combined sources
Beta strandi123 – 13513Combined sources
Beta strandi139 – 1424Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi157 – 1615Combined sources
Helixi164 – 1696Combined sources
Beta strandi177 – 1826Combined sources
Helixi184 – 1863Combined sources
Beta strandi188 – 1914Combined sources
Helixi193 – 1975Combined sources
Beta strandi199 – 21214Combined sources
Beta strandi214 – 2229Combined sources
Turni224 – 2263Combined sources
Beta strandi228 – 2347Combined sources
Helixi235 – 2384Combined sources
Beta strandi246 – 2516Combined sources
Helixi253 – 2553Combined sources
Beta strandi257 – 2615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9MX-ray1.75A/B1-262[»]
1B9NX-ray2.09A/B1-262[»]
1H9RX-ray1.90A/B124-262[»]
1H9SX-ray1.82A/B124-262[»]
1O7LX-ray2.75A/B/C/D1-262[»]
ProteinModelPortaliP0A9G8.
SMRiP0A9G8. Positions 1-262.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9G8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 121121IAdd
BLAST
Regioni122 – 18362IIA (MOP1A)Add
BLAST
Regioni125 – 1339Required for dimer formation and molybdate binding
Regioni184 – 25572IIB (MOP2)Add
BLAST
Regioni256 – 2627IIA (MOP1B)

Domaini

Contains two major domains: the N-terminal domain I forms a winged helix-turn-helix motif and interacts with DNA. The C-terminal domain II is the putative molybdate-binding component and contains a tandem repeat of the Mop domain, each of which forms a beta-barrel. 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.

Sequence similaritiesi

Belongs to the ModE family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105F4R. Bacteria.
COG2005. LUCA.
HOGENOMiHOG000156225.
InParanoidiP0A9G8.
KOiK02019.
OMAiSYKTAWH.
OrthoDBiEOG68Q0VP.
PhylomeDBiP0A9G8.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR004606. Mo-pterin-bd.
IPR008995. Mo/tungstate-bd_C_term_dom.
IPR016462. ModE.
IPR003725. ModE-bd_N.
IPR005116. Transp-assoc_OB_typ1.
IPR000847. Tscrpt_reg_HTH_LysR.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00126. HTH_1. 1 hit.
PF03459. TOBE. 2 hits.
[Graphical view]
PIRSFiPIRSF005763. Txn_reg_ModE. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50331. SSF50331. 2 hits.
TIGRFAMsiTIGR00637. ModE_repress. 1 hit.
TIGR00638. Mop. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A9G8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAEILLTLK LQQKLFADPR RISLLKHIAL SGSISQGAKD AGISYKSAWD
60 70 80 90 100
AINEMNQLSE HILVERATGG KGGGGAVLTR YGQRLIQLYD LLAQIQQKAF
110 120 130 140 150
DVLSDDDALP LNSLLAAISR FSLQTSARNQ WFGTITARDH DDVQQHVDVL
160 170 180 190 200
LADGKTRLKV AITAQSGARL GLDEGKEVLI LLKAPWVGIT QDEAVAQNAD
210 220 230 240 250
NQLPGIISHI ERGAEQCEVL MALPDGQTLC ATVPVNEATS LQQGQNVTAY
260
FNADSVIIAT LC
Length:262
Mass (Da):28,281
Last modified:July 19, 2005 - v1
Checksum:i9A17636162F4233E
GO

Mass spectrometryi

Molecular mass is 28271 Da from positions 1 - 262. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07867 Genomic DNA. Translation: AAB06892.1.
U27192 Genomic DNA. Translation: AAB60175.1.
U34275 Genomic DNA. Translation: AAA77051.1.
U00096 Genomic DNA. Translation: AAC73848.1.
AP009048 Genomic DNA. Translation: BAA35425.1.
PIRiJC6037.
RefSeqiNP_415282.1. NC_000913.3.
WP_001147439.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73848; AAC73848; b0761.
BAA35425; BAA35425; BAA35425.
GeneIDi945366.
KEGGiecj:JW0744.
eco:b0761.
PATRICi32116723. VBIEscCol129921_0787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07867 Genomic DNA. Translation: AAB06892.1.
U27192 Genomic DNA. Translation: AAB60175.1.
U34275 Genomic DNA. Translation: AAA77051.1.
U00096 Genomic DNA. Translation: AAC73848.1.
AP009048 Genomic DNA. Translation: BAA35425.1.
PIRiJC6037.
RefSeqiNP_415282.1. NC_000913.3.
WP_001147439.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9MX-ray1.75A/B1-262[»]
1B9NX-ray2.09A/B1-262[»]
1H9RX-ray1.90A/B124-262[»]
1H9SX-ray1.82A/B124-262[»]
1O7LX-ray2.75A/B/C/D1-262[»]
ProteinModelPortaliP0A9G8.
SMRiP0A9G8. Positions 1-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259327. 4 interactions.
DIPiDIP-10238N.
IntActiP0A9G8. 1 interaction.
STRINGi511145.b0761.

Proteomic databases

PaxDbiP0A9G8.
PRIDEiP0A9G8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73848; AAC73848; b0761.
BAA35425; BAA35425; BAA35425.
GeneIDi945366.
KEGGiecj:JW0744.
eco:b0761.
PATRICi32116723. VBIEscCol129921_0787.

Organism-specific databases

EchoBASEiEB3017.
EcoGeneiEG13227. modE.

Phylogenomic databases

eggNOGiENOG4105F4R. Bacteria.
COG2005. LUCA.
HOGENOMiHOG000156225.
InParanoidiP0A9G8.
KOiK02019.
OMAiSYKTAWH.
OrthoDBiEOG68Q0VP.
PhylomeDBiP0A9G8.

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-185.
ECOL316407:JW0744-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A9G8.
PROiP0A9G8.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR004606. Mo-pterin-bd.
IPR008995. Mo/tungstate-bd_C_term_dom.
IPR016462. ModE.
IPR003725. ModE-bd_N.
IPR005116. Transp-assoc_OB_typ1.
IPR000847. Tscrpt_reg_HTH_LysR.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00126. HTH_1. 1 hit.
PF03459. TOBE. 2 hits.
[Graphical view]
PIRSFiPIRSF005763. Txn_reg_ModE. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50331. SSF50331. 2 hits.
TIGRFAMsiTIGR00637. ModE_repress. 1 hit.
TIGR00638. Mop. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene."
    Walkenhorst H.M., Hemschemeier S.K., Eichenlaub R.
    Microbiol. Res. 150:347-361(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / MC1000 / ATCC 39531.
  2. "Repression of the Escherichia coli modABCD (molybdate transport) operon by ModE."
    Grunden A.M., Ray R.M., Rosentel J.K., Healy F.G., Shanmugam K.T.
    J. Bacteriol. 178:735-744(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12, MASS SPECTROMETRY, MUTAGENESIS OF ALA-76; THR-125; GLY-133 AND GLN-216.
    Strain: K12.
  3. "Sequence spanning gap between Genbank entries L34009 and X69182."
    Kim K., Allen E., Araujo R., Aparicio A., Botstein D., Cherry M., Chung E., Dietrich F., Duncan M., Federspiel N., Kalman S., Komp C., Lashkari D., Lew H., Lin D., Namath A., Oefner P., Davis R.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli."
    Anderson L.A., Palmer T., Price N.C., Bornemann S., Boxer D.H., Pau R.N.
    Eur. J. Biochem. 246:119-126(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds."
    Hall D.R., Gourley D.G., Leonard G.A., Duke E.M.H., Anderson L.A., Boxer D.H., Hunter W.N.
    EMBO J. 18:1435-1446(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
  9. Cited for: REVIEW.

Entry informationi

Entry nameiMODE_ECOLI
AccessioniPrimary (citable) accession number: P0A9G8
Secondary accession number(s): P46930
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: January 20, 2016
This is version 98 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, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.