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ftsY signal recognition particle receptor [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947978, updated on 17-Dec-2024

Summary

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Official Symbol
ftsY
Official Full Name
signal recognition particle receptor
Primary source
ECOCYC:EG10346
Locus tag
b3464
See related
ASAP:ABE-0011318
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
ECK3448
Summary
FtsY is found as both membrane-associated isoforms and as shorter soluble isoforms which are lacking the N-terminal 14 aa; FtsY is attached to the cytoplasmic membrane by its association with the secYEG translocon and the FtsY N-terminal 14 aa cleavable membrane anchor facilitates this association by first transiently anchoring FtsY to the membrane (Luirink, 1994; Weiche, 2008). [More information is available at EcoGene: EG10346].
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Genomic context

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Sequence:
NC_000913.3 (3602750..3604243, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene RNA polymerase sigma factor RpoH Neighboring gene cell division protein FtsX Neighboring gene cell division protein FtsE Neighboring gene 16S rRNA m(2)G966 methyltransferase Neighboring gene DUF1145 domain-containing protein YhhL Neighboring gene DUF2500 domain-containing protein YhhM

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. Structural insights into the G-loop dynamics of E. coli FtsY NG domain. Faoro C, et al. J Struct Biol, 2019 Dec 1. PMID 31520694
  2. The functioning of the SRP receptor FtsY in protein-targeting in E. coli is correlated with its ability to bind and hydrolyse GTP. Kusters R, et al. FEBS Lett, 1995 Sep 25. PMID 7556679
  3. An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY. Luirink J, et al. EMBO J, 1994 May 15. PMID 8194520, Free PMC Article
  4. FtsY, the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins. Seluanov A, et al. J Biol Chem, 1997 Jan 24. PMID 8999901
  5. Membrane association of FtsY, the E. coli SRP receptor. de Leeuw E, et al. FEBS Lett, 1997 Oct 27. PMID 9373157

See all (101) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. A nucleotide sensing function of the P-loop assists FtsY in nucleotide-binding.The binding of magnesium in the nucleotide site causes the reorientation of the beta- and gamma- phosphate groups toward the jaws of the P-loop and stabilizes the binding of the nucleotide, creating a network of hydrogen and water-bridge interactions in FtsY structure.
    Title: Structural insights into the G-loop dynamics of E. coli FtsY NG domain.
  2. FtsY can target the membrane co-translationally.
    Title: Co-translational membrane association of the Escherichia coli SRP receptor.
  3. analysis of the ribosome-SRP-FtsY cotranslational targeting complex in the closed state
    Title: Ribosome-SRP-FtsY cotranslational targeting complex in the closed state.
  4. 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.
  5. Data show that FtsY, the bacterial SRalpha homologue, binds to the exposed C4/C5 loops of SecY, the central component of the bacterial Sec translocon, and that the same loops serve also as binding sites for SecA and the ribosome.
    Title: The bacterial SRP receptor, SecA and the ribosome use overlapping binding sites on the SecY translocon.
  6. 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.
  7. 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.
  8. Data show that phospholipid binding drives important conformational rearrangements that activate the bacterial SRP receptor FtsY and the SRP-FtsY complex.
    Title: Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.
  9. Data showed that FtsY depletion inhibits the translation of both SRP-dependent and independent proteins. This synthesis defect is the result of a multifaceted response that includes the upregulation of the ribosome-inactivating protein RMF.
    Title: Depletion of the signal recognition particle receptor inactivates ribosomes in Escherichia coli.
  10. The data reveal that the two consecutive lipid-binding helices of FtsY can provide a membrane contact that does not differ significantly in stability from that provided by a transmembrane domain.
    Title: Two cooperating helices constitute the lipid-binding domain of the bacterial SRP receptor.
Submit: New GeneRIF Correction See all GeneRIFs (16)

Pathways from PubChem

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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 ATP hydrolysis activity IEA
Inferred from Electronic Annotation
more info
  
enables GTP binding IEA
Inferred from Electronic Annotation
more info
  
enables GTPase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables GTPase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables GTPase activity 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 
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables signal recognition particle binding IBA
Inferred from Biological aspect of Ancestor
more info
  
Process Evidence Code Pubs
involved_in SRP-dependent cotranslational protein targeting to membrane IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in SRP-dependent cotranslational protein targeting to membrane IEA
Inferred from Electronic Annotation
more info
  
involved_in protein targeting IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein targeting to membrane IEA
Inferred from Electronic Annotation
more info
  
involved_in stringent response IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytoplasmic side of plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
is_active_in plasma membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
signal recognition particle receptor

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
    3602750..3604243 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417921.1 signal recognition particle receptor [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417921.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    W1WW58
    Conserved Domains (2) summary
    PRK10416
    Location:186 → 497
    PRK10416; signal recognition particle-docking protein FtsY; Provisional
    PRK10811
    Location:21 → 187
    rne; ribonuclease E; Reviewed
Nucleotide Protein
Heading Accession and Version

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