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ffh signal recognition particle protein component [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947102, updated on 3-Dec-2024

Summary

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Official Symbol
ffh
Official Full Name
signal recognition particle protein component
Primary source
ECOCYC:EG10300
Locus tag
b2610
See related
ASAP:ABE-0008586
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
ECK2607
Summary
Binds nascent signal peptides, GTP and 4.5S RNA. [More information is available at EcoGene: EG10300].
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Genomic context

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Sequence:
NC_000913.3 (2746434..2747795, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ribosome maturation factor RimM Neighboring gene 30S ribosomal subunit protein S16 Neighboring gene cytochrome c assembly family protein Neighboring gene UPF0053 family inner membrane protein YfjD

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. Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence. Mercier E, et al. Nucleic Acids Res, 2017 Nov 16. PMID 29149347, Free PMC Article
  2. Signal peptides bind and aggregate RNA. An alternative explanation for GTPase inhibition in the signal recognition particle. Swain JF, et al. J Biol Chem, 2001 Apr 13. PMID 11148214
  3. Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog. Bernstein HD, et al. Proc Natl Acad Sci U S A, 1993 Jun 1. PMID 8389475, Free PMC Article
  4. The GTPase activity of the Escherichia coli Ffh protein is important for normal growth. Samuelsson T, et al. Biochim Biophys Acta, 1995 Jun 20. PMID 7612669
  5. Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methods. Clérico EM, et al. Biopolymers, 2009. PMID 19280642, Free PMC Article

See all (119) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Lon Protease Removes Excess Signal Recognition Particle Protein in Escherichia coli.
    Title: Lon Protease Removes Excess Signal Recognition Particle Protein in Escherichia coli.
  2. Here, theauthors show that the C-terminal helix of the signal-sequence-binding domain of signal recognition particle penetrates into the ribosomal tunnel and contacts the intra-tunnel loop of ribosomal protein uL23.
    Title: The signal recognition particle contacts uL23 and scans substrate translation inside the ribosomal tunnel.
  3. The kinetic analysis indicate that, at cellular concentrations of ribosomes and signal recognition particle (SRP), signal-anchor sequence (SAS) rapidly binds to translating ribosomes prior to the emergence of an SAS and forms an initial complex that rapidly rearranges to a more stable engaged complex.
    Title: Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence.
  4. Data indicate that the sigma factor 32 (sigma32)-Ffh (the protein subunit of signal recognition particle (SRP) interaction was significantly affected by mutations in this region that compromise the feedback regulation.
    Title: A Novel SRP Recognition Sequence in the Homeostatic Control Region of Heat Shock Transcription Factor σ32.
  5. The cryo-electron microscopy structure of this 'false' early complex with EspP revealed an ordered M domain of SRP protein Ffh making two ribosomal contacts, and the NG domains of Ffh and FtsY forming a distorted, flexible heterodimer.
    Title: Structural basis of signal sequence surveillance and selection by the SRP-FtsY complex.
  6. Data indicate that Escherichia coli Ffh protein bound to the large subunit of mitochondrial ribosomes, and could relieve, to some degree, the defect of Saccharomyces cerevisiae Oxa1 mutants.
    Title: Partial suppression of Oxa1 mutants by mitochondria-targeted signal recognition particle provides insights into the evolution of the cotranslational insertion systems.
  7. Overexpression the M domain of Ffh inhibits the expression of membrane proteins.
    Title: Escherichia coli SRP, its protein subunit Ffh, and the Ffh M domain are able to selectively limit membrane protein expression when overexpressed.
  8. crystal structure of the SRP:SR complex at 3.9 angstrom resolution and biochemical data revealing that the activated SRP:SR GTPase complex binds the distal end of the SRP hairpin RNA where GTP hydrolysis is stimulated
    Title: The crystal structure of the signal recognition particle in complex with its receptor.
  9. Results suggest that indeed, while FtsY-depletion affects earlier steps in the pathway (possibly translation), Ffh-depletion disrupts membrane protein biogenesis later during the targeting pathway by preventing their functional assembly in the membrane.
    Title: Membrane protein biogenesis in Ffh- or FtsY-depleted Escherichia coli.
  10. the SRP and SR GTPases, without recruiting external regulatory factors, constitute a self-sufficient system that provides exquisite spatial and temporal control of a complex cellular process
    Title: Multiple conformational switches in a GTPase complex control co-translational protein targeting.
Submit: New GeneRIF Correction See all GeneRIFs (16)

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables 7S RNA binding IEA
Inferred from Electronic Annotation
more info
  
enables ATP hydrolysis activity IEA
Inferred from Electronic Annotation
more info
  
enables GTP binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables GTP binding IEA
Inferred from Electronic Annotation
more info
  
enables GTP binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
contributes_to GTPase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables GTPase activity IEA
Inferred from Electronic Annotation
more info
  
enables GTPase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables RNA binding IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in SRP-dependent cotranslational protein targeting to membrane IEA
Inferred from Electronic Annotation
more info
  
involved_in protein targeting to membrane IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within protein targeting to membrane IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
part_of ribonucleoprotein complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of signal recognition particle IEA
Inferred from Electronic Annotation
more info
  
part_of signal recognition particle IMP
Inferred from Mutant Phenotype
more info
 PubMed 

General protein information

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Preferred Names
signal recognition particle protein component

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
    2746434..2747795 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417101.1 signal recognition particle protein component [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417101.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A2W6PI73
    Conserved Domains (1) summary
    PRK10867
    Location:1 → 425
    PRK10867; signal recognition particle protein; Provisional
Nucleotide Protein
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