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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
    Heading Accession and Version

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