A0A3T4RMW8 · A0A3T4RMW8_SALET
- ProteinSignal recognition particle receptor FtsY
- GeneftsY
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids491 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.
Catalytic activity
- GTP + H2O = GDP + H+ + phosphate
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Biological Process | SRP-dependent cotranslational protein targeting to membrane |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSignal recognition particle receptor FtsY
- EC number
- Short namesSRP receptor
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionA0A3T4RMW8
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Membrane ; Peripheral membrane protein
Keywords
- Cellular component
Interaction
Subunit
Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY. SRP is a ribonucleoprotein composed of Ffh and a 4.5S RNA molecule.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-58 | Disordered | ||||
Sequence: MAKQKKRGFFSWLGFGDKEQKQEQTEEQQIVEEQRPVEPPVETAADIDAQTPAHSKAE | ||||||
Compositional bias | 19-33 | Basic and acidic residues | ||||
Sequence: EQKQEQTEEQQIVEE | ||||||
Region | 70-89 | Disordered | ||||
Sequence: TEKVQESEKPQPVEPEPATA | ||||||
Domain | 461-474 | SRP54-type proteins GTP-binding | ||||
Sequence: PIRYIGVGERIEDL |
Domain
Contains an acidic N-terminal A domain, a central N domain and a C-terminal GTPase G domain that can bind and hydrolyze GTP. Contains at least two lipid-binding sites. The first site contains the first 14 amino acids (helix 1) and the second binding site is an amphipathic alpha-helix located at the interface between the A- and the N-domain (helix 2).
Sequence similarities
Belongs to the GTP-binding SRP family. FtsY subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length491
- Mass (Da)53,777
- Last updated2019-05-08 v1
- Checksum1D43F7DB77B2D8E3
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 19-33 | Basic and acidic residues | ||||
Sequence: EQKQEQTEEQQIVEE |