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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)DescriptionActionsGraphical viewLength
DNA bindingi33 – 79H-T-H motifAdd BLAST47

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi76A → V: Partial loss of repression by ModE. 1 Publication1
Mutagenesisi125T → I: Transcription repression by ModE even in the absence of molybdate. 1 Publication1
Mutagenesisi133G → D: Transcription repression by ModE even in the absence of molybdate. 1 Publication1
Mutagenesisi216 – 262Missing : Transcription repression by ModE even in the absence of molybdate. Add BLAST47

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002011251 – 262Transcriptional regulator ModEAdd BLAST262

Proteomic databases

PaxDbiP0A9G8.
PRIDEiP0A9G8.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4259327. 4 interactors.
DIPiDIP-10238N.
IntActiP0A9G8. 1 interactor.
STRINGi511145.b0761.

Structurei

Secondary structure

1262
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 11Combined sources8
Beta strandi14 – 17Combined sources4
Helixi19 – 31Combined sources13
Helixi34 – 41Combined sources8
Helixi45 – 59Combined sources15
Beta strandi64 – 66Combined sources3
Beta strandi76 – 78Combined sources3
Helixi80 – 105Combined sources26
Helixi114 – 121Combined sources8
Beta strandi123 – 135Combined sources13
Beta strandi139 – 142Combined sources4
Beta strandi145 – 151Combined sources7
Beta strandi157 – 161Combined sources5
Helixi164 – 169Combined sources6
Beta strandi177 – 182Combined sources6
Helixi184 – 186Combined sources3
Beta strandi188 – 191Combined sources4
Helixi193 – 197Combined sources5
Beta strandi199 – 212Combined sources14
Beta strandi214 – 222Combined sources9
Turni224 – 226Combined sources3
Beta strandi228 – 234Combined sources7
Helixi235 – 238Combined sources4
Beta strandi246 – 251Combined sources6
Helixi253 – 255Combined sources3
Beta strandi257 – 261Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9G8.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 121IAdd BLAST121
Regioni122 – 183IIA (MOP1A)Add BLAST62
Regioni125 – 133Required for dimer formation and molybdate binding9
Regioni184 – 255IIB (MOP2)Add BLAST72
Regioni256 – 262IIA (MOP1B)7

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.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259327. 4 interactors.
DIPiDIP-10238N.
IntActiP0A9G8. 1 interactor.
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.
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...

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: November 2, 2016
This is version 100 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.