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

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_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
FtsY can target the membrane co-translationally.
Title: Co-translational membrane association of the Escherichia coli SRP receptor.
analysis of the ribosome-SRP-FtsY cotranslational targeting complex in the closed state
Title: Ribosome-SRP-FtsY cotranslational targeting complex in the closed state.
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.
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.
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.
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.
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.
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.
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

Orthologs from OrthoDB

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

NC_000913.3 Reference assembly

Range

3602750..3604243 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

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