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Protein

HTH-type transcriptional regulator TreR

Gene

treR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Repressor of the treBC operon. Binds trehalose 6-phosphate as an inducer.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi7 – 2620H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • transcription factor activity, sequence-specific DNA binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12202-MONOMER.
ECOL316407:JW4200-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional regulator TreR
Alternative name(s):
Trehalose operon repressor
Gene namesi
Name:treR
Ordered Locus Names:b4241, JW4200
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12202. treR.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315HTH-type transcriptional regulator TreRPRO_0000108005Add
BLAST

Proteomic databases

PaxDbiP36673.
PRIDEiP36673.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4260956. 9 interactions.
DIPiDIP-11026N.
IntActiP36673. 10 interactions.
STRINGi511145.b4241.

Structurei

Secondary structure

1
315
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi64 – 707Combined sources
Helixi75 – 9117Combined sources
Beta strandi94 – 996Combined sources
Helixi104 – 11613Combined sources
Beta strandi120 – 1256Combined sources
Turni132 – 1354Combined sources
Helixi136 – 1383Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi152 – 1576Combined sources
Helixi159 – 17214Combined sources
Beta strandi178 – 1814Combined sources
Turni188 – 1914Combined sources
Helixi192 – 20413Combined sources
Beta strandi210 – 2123Combined sources
Helixi218 – 2247Combined sources
Helixi225 – 2284Combined sources
Beta strandi235 – 2406Combined sources
Helixi241 – 25313Combined sources
Beta strandi260 – 2645Combined sources
Helixi268 – 2736Combined sources
Beta strandi277 – 2815Combined sources
Helixi284 – 29916Combined sources
Beta strandi307 – 3104Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XXHX-ray2.40A/B61-315[»]
ProteinModelPortaliP36673.
SMRiP36673. Positions 5-315.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36673.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 5955HTH lacI-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH lacI-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105D4X. Bacteria.
COG1609. LUCA.
HOGENOMiHOG000283706.
KOiK03485.
OMAiFGFTGCD.
OrthoDBiEOG6SJJMM.
PhylomeDBiP36673.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR010982. Lambda_DNA-bd_dom.
IPR028082. Peripla_BP_I.
IPR012771. Trehalos_R_gpbac.
IPR000843. Tscrpt_reg_HTH_LacI.
[Graphical view]
PfamiPF00356. LacI. 1 hit.
[Graphical view]
PRINTSiPR00036. HTHLACI.
SMARTiSM00354. HTH_LACI. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
SSF53822. SSF53822. 1 hit.
TIGRFAMsiTIGR02405. trehalos_R_Ecol. 1 hit.
PROSITEiPS00356. HTH_LACI_1. 1 hit.
PS50932. HTH_LACI_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36673-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQNRLTIKDI ARLSGVGKST VSRVLNNESG VSQLTRERVE AVMNQHGFSP
60 70 80 90 100
SRSARAMRGQ SDKVVAIIVT RLDSLSENLA VQTMLPAFYE QGYDPIMMES
110 120 130 140 150
QFSPQLVAEH LGVLKRRNID GVVLFGFTGI TEEMLAHWQS SLVLLARDAK
160 170 180 190 200
GFASVCYDDE GAIKILMQRL YDQGHRNISY LGVPHSDVTT GKRRHEAYLA
210 220 230 240 250
FCKAHKLHPV AALPGLAMKQ GYENVAKVIT PETTALLCAT DTLALGASKY
260 270 280 290 300
LQEQRIDTLQ LASVGNTPLM KFLHPEIVTV DPGYAEAGRQ AACQLIAQVT
310
GRSEPQQIII PATLS
Length:315
Mass (Da):34,531
Last modified:February 1, 1995 - v2
Checksum:i16C528EBDE40C665
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07790 Unassigned DNA. Translation: AAB47715.1.
U14003 Genomic DNA. Translation: AAA97138.1.
U00096 Genomic DNA. Translation: AAC77198.1.
AP009048 Genomic DNA. Translation: BAE78240.1.
U06195 Genomic DNA. No translation available.
PIRiS56467.
RefSeqiNP_418662.1. NC_000913.3.
WP_001181307.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77198; AAC77198; b4241.
BAE78240; BAE78240; BAE78240.
GeneIDi948760.
KEGGiecj:JW4200.
eco:b4241.
PATRICi32124057. VBIEscCol129921_4373.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07790 Unassigned DNA. Translation: AAB47715.1.
U14003 Genomic DNA. Translation: AAA97138.1.
U00096 Genomic DNA. Translation: AAC77198.1.
AP009048 Genomic DNA. Translation: BAE78240.1.
U06195 Genomic DNA. No translation available.
PIRiS56467.
RefSeqiNP_418662.1. NC_000913.3.
WP_001181307.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XXHX-ray2.40A/B61-315[»]
ProteinModelPortaliP36673.
SMRiP36673. Positions 5-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260956. 9 interactions.
DIPiDIP-11026N.
IntActiP36673. 10 interactions.
STRINGi511145.b4241.

Proteomic databases

PaxDbiP36673.
PRIDEiP36673.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77198; AAC77198; b4241.
BAE78240; BAE78240; BAE78240.
GeneIDi948760.
KEGGiecj:JW4200.
eco:b4241.
PATRICi32124057. VBIEscCol129921_4373.

Organism-specific databases

EchoBASEiEB2118.
EcoGeneiEG12202. treR.

Phylogenomic databases

eggNOGiENOG4105D4X. Bacteria.
COG1609. LUCA.
HOGENOMiHOG000283706.
KOiK03485.
OMAiFGFTGCD.
OrthoDBiEOG6SJJMM.
PhylomeDBiP36673.

Enzyme and pathway databases

BioCyciEcoCyc:EG12202-MONOMER.
ECOL316407:JW4200-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP36673.
PROiP36673.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR010982. Lambda_DNA-bd_dom.
IPR028082. Peripla_BP_I.
IPR012771. Trehalos_R_gpbac.
IPR000843. Tscrpt_reg_HTH_LacI.
[Graphical view]
PfamiPF00356. LacI. 1 hit.
[Graphical view]
PRINTSiPR00036. HTHLACI.
SMARTiSM00354. HTH_LACI. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
SSF53822. SSF53822. 1 hit.
TIGRFAMsiTIGR02405. trehalos_R_Ecol. 1 hit.
PROSITEiPS00356. HTH_LACI_1. 1 hit.
PS50932. HTH_LACI_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of TreR, the major regulator of the Escherichia coli trehalose system."
    Horlacher R., Boos W.
    J. Biol. Chem. 272:13026-13032(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: K12.
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Molecular analysis of treB encoding the Escherichia coli enzyme II specific for trehalose."
    Klein W., Horlacher R., Boos W.
    J. Bacteriol. 177:4043-4052(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 307-315.
    Strain: K12.
  6. "Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose."
    Hars U., Horlacher R., Boos W., Welte W., Diederichs K.
    Protein Sci. 7:2511-2521(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiTRER_ECOLI
AccessioniPrimary (citable) accession number: P36673
Secondary accession number(s): Q2M666
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1995
Last modified: January 20, 2016
This is version 136 of the entry and version 2 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. 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.