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hfq [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948689, updated on 11-Sep-2024

Summary

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Official Symbol
hfq
Primary source
ECOCYC:EG10438
Locus tag
b4172
See related
ASAP:ABE-0013659
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK4168
Summary
The C-terminal of Hfq is not necessary for hexamerization. [More information is available at EcoGene: EG10438]. Hfq is an RNA-binding protein that stimulates RNA-RNA pairing and affects many cellular processes, similar to mammalian Sm/Sm-like proteins . [More information is available at EcoCyc: EG10438].
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Genomic context

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Sequence:
NC_000913.3 (4400288..4400596)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene N-acetylmuramoyl-L-alanine amidase B Neighboring gene DNA mismatch repair protein MutL Neighboring gene tRNA dimethylallyltransferase Neighboring gene ribosome rescue factor HflX Neighboring gene regulator of FtsH protease

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Multiple in vivo roles for the C-terminal domain of the RNA chaperone Hfq. Kavita K, et al. Nucleic Acids Res, 2022 Feb 22. PMID 35104863, Free PMC Article
  2. Optimization of a bacterial three-hybrid assay through in vivo titration of an RNA-DNA adapter protein. Wang CD, et al. RNA, 2021 Apr. PMID 33500316, Free PMC Article
  3. The RNA-binding protein Hfq assembles into foci-like structures in nitrogen starved Escherichia coli. McQuail J, et al. J Biol Chem, 2020 Aug 28. PMID 32532816, Free PMC Article
  4. Hfq CLASH uncovers sRNA-target interaction networks linked to nutrient availability adaptation. Iosub IA, et al. Elife, 2020 May 1. PMID 32356726, Free PMC Article
  5. Crystal structure of an Escherichia coli Hfq Core (residues 2-69)-DNA complex reveals multifunctional nucleic acid binding sites. Orans J, et al. Nucleic Acids Res, 2020 Apr 17. PMID 32133526, Free PMC Article

See all (190) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Synthesis of the NarP response regulator of nitrate respiration in Escherichia coli is regulated at multiple levels by Hfq and small RNAs.
    Title: Synthesis of the NarP response regulator of nitrate respiration in Escherichia coli is regulated at multiple levels by Hfq and small RNAs.
  2. Multiple in vivo roles for the C-terminal domain of the RNA chaperone Hfq.
    Title: Multiple in vivo roles for the C-terminal domain of the RNA chaperone Hfq.
  3. The association between Hfq and RNase E in long-term nitrogen-starved Escherichia coli.
    Title: The association between Hfq and RNase E in long-term nitrogen-starved Escherichia coli.
  4. Hfq and RNase R Mediate rRNA Processing and Degradation in a Novel RNA Quality Control Process.
    Title: Hfq and RNase R Mediate rRNA Processing and Degradation in a Novel RNA Quality Control Process.
  5. Translation inhibition from a distance: The small RNA SgrS silences a ribosomal protein S1-dependent enhancer.
    Title: Translation inhibition from a distance: The small RNA SgrS silences a ribosomal protein S1-dependent enhancer.
  6. RNA binding of Hfq monomers promotes RelA-mediated hexamerization in a limiting Hfq environment.
    Title: RNA binding of Hfq monomers promotes RelA-mediated hexamerization in a limiting Hfq environment.
  7. Optimization of a bacterial three-hybrid assay through in vivo titration of an RNA-DNA adapter protein.
    Title: Optimization of a bacterial three-hybrid assay through in vivo titration of an RNA-DNA adapter protein.
  8. Hfq CLASH uncovers sRNA-target interaction networks linked to nutrient availability adaptation.
    Title: Hfq CLASH uncovers sRNA-target interaction networks linked to nutrient availability adaptation.
  9. The RNA-binding protein Hfq assembles into foci-like structures in nitrogen starved Escherichia coli.
    Title: The RNA-binding protein Hfq assembles into foci-like structures in nitrogen starved Escherichia coli.
  10. Structure studies of an Escherichia coli Hfq Core and DNA complex reveals multifunctional binding sites.
    Title: Crystal structure of an Escherichia coli Hfq Core (residues 2-69)-DNA complex reveals multifunctional nucleic acid binding sites.
Submit: New GeneRIF Correction See all GeneRIFs (78)

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables DNA binding EXP
Inferred from Experiment
more info
 PubMed 
enables DNA binding IEA
Inferred from Electronic Annotation
more info
  
enables RNA binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables RNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables RNA binding IEA
Inferred from Electronic Annotation
more info
  
enables RNA folding chaperone EXP
Inferred from Experiment
more info
 PubMed 
enables bent DNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables tRNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in RNA folding IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within positive regulation of translation, ncRNA-mediated IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulation of DNA-templated transcription IEA
Inferred from Electronic Annotation
more info
  
involved_in regulation of RNA stability IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in regulation of translation, ncRNA-mediated IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within sRNA-mediated post-transcriptional gene silencing IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in tRNA processing IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in bacterial nucleoid IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
RNA-binding protein Hfq

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    4400288..4400596
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418593.1 RNA-binding protein Hfq [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418593.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A376VR90
    Conserved Domains (1) summary
    PRK00395
    Location:1 → 76
    hfq; RNA-binding protein Hfq; Provisional
Nucleotide Protein
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