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Protein

Transcriptional regulatory protein YehT

Gene

yehT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Member of the two-component regulatory system YehU/YehT, which may be involved in the stationary-phase control network. Regulates expression of yjiY by binding to its promoter region.2 Publications

GO - Molecular functioni

GO - Biological processi

  • phosphorelay signal transduction system Source: EcoCyc
  • regulation of transcription, DNA-templated Source: EcoCyc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Two-component regulatory system

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12006-MONOMER.
ECOL316407:JW5352-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulatory protein YehT
Gene namesi
Name:yehT
Ordered Locus Names:b2125, JW5352
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12006. yehT.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: GOC
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Deletion of yehUT has no obvious phenotypic effect under the conditions tested.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541D → E: 2-fold increase in yjiY induction. 1 Publication
Mutagenesisi54 – 541D → N: 10-fold decrease in yjiY induction. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239Transcriptional regulatory protein YehTPRO_0000081361Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 5414-aspartylphosphatePROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated by YehU.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0AFT5.
PRIDEiP0AFT5.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
sfsAP0A8232EBI-556431,EBI-556413

Protein-protein interaction databases

BioGridi4261849. 319 interactions.
DIPiDIP-48085N.
IntActiP0AFT5. 3 interactions.
MINTiMINT-1311507.
STRINGi511145.b2125.

Structurei

3D structure databases

ProteinModelPortaliP0AFT5.
SMRiP0AFT5. Positions 2-122, 135-239.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 116114Response regulatoryPROSITE-ProRule annotationAdd
BLAST
Domaini137 – 239103HTH LytTR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH LytTR-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108NEV. Bacteria.
COG3279. LUCA.
HOGENOMiHOG000242207.
InParanoidiP0AFT5.
KOiK02477.
OMAiHDAFALR.
OrthoDBiEOG64R63J.
PhylomeDBiP0AFT5.

Family and domain databases

InterProiIPR011006. CheY-like_superfamily.
IPR007492. LytTR_DNA-bd_dom.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF04397. LytTR. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00850. LytTR. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS50930. HTH_LYTTR. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AFT5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKVLIVDDE PLARENLRVF LQEQSDIEIV GECSNAVEGI GAVHKLRPDV
60 70 80 90 100
LFLDIQMPRI SGLEMVGMLD PEHRPYIVFL TAFDEYAIKA FEEHAFDYLL
110 120 130 140 150
KPIDEARLEK TLARLRQERS KQDVSLLPEN QQALKFIPCT GHSRIYLLQM
160 170 180 190 200
KDVAFVSSRM SGVYVTSHEG KEGFTELTLR TLESRTPLLR CHRQYLVNLA
210 220 230
HLQEIRLEDN GQAELILRNG LTVPVSRRYL KSLKEAIGL
Length:239
Mass (Da):27,400
Last modified:December 20, 2005 - v1
Checksum:i5665AAE782B7FBA3
GO

Sequence cautioni

The sequence AAA60488.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00007 Genomic DNA. Translation: AAA60488.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75186.2.
AP009048 Genomic DNA. Translation: BAE76601.1.
PIRiD64980.
RefSeqiNP_416629.4. NC_000913.3.
WP_000598641.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75186; AAC75186; b2125.
BAE76601; BAE76601; BAE76601.
GeneIDi949024.
KEGGiecj:JW5352.
eco:b2125.
PATRICi32119587. VBIEscCol129921_2204.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00007 Genomic DNA. Translation: AAA60488.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75186.2.
AP009048 Genomic DNA. Translation: BAE76601.1.
PIRiD64980.
RefSeqiNP_416629.4. NC_000913.3.
WP_000598641.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AFT5.
SMRiP0AFT5. Positions 2-122, 135-239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261849. 319 interactions.
DIPiDIP-48085N.
IntActiP0AFT5. 3 interactions.
MINTiMINT-1311507.
STRINGi511145.b2125.

Proteomic databases

PaxDbiP0AFT5.
PRIDEiP0AFT5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75186; AAC75186; b2125.
BAE76601; BAE76601; BAE76601.
GeneIDi949024.
KEGGiecj:JW5352.
eco:b2125.
PATRICi32119587. VBIEscCol129921_2204.

Organism-specific databases

EchoBASEiEB1944.
EcoGeneiEG12006. yehT.

Phylogenomic databases

eggNOGiENOG4108NEV. Bacteria.
COG3279. LUCA.
HOGENOMiHOG000242207.
InParanoidiP0AFT5.
KOiK02477.
OMAiHDAFALR.
OrthoDBiEOG64R63J.
PhylomeDBiP0AFT5.

Enzyme and pathway databases

BioCyciEcoCyc:EG12006-MONOMER.
ECOL316407:JW5352-MONOMER.

Miscellaneous databases

PROiP0AFT5.

Family and domain databases

InterProiIPR011006. CheY-like_superfamily.
IPR007492. LytTR_DNA-bd_dom.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF04397. LytTR. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00850. LytTR. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS50930. HTH_LYTTR. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Automated multiplex sequencing of the E.coli genome."
    Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / BHB2600.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli."
    Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., Ishihama A.
    J. Biol. Chem. 280:1448-1456(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "First insights into the unexplored two-component system YehU/YehT in Escherichia coli."
    Kraxenberger T., Fried L., Behr S., Jung K.
    J. Bacteriol. 194:4272-4284(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-54.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiYEHT_ECOLI
AccessioniPrimary (citable) accession number: P0AFT5
Secondary accession number(s): P33356
, P76432, P76433, Q2MAV5, Q9ALR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 20, 2016
This is version 88 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

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.