STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ftsYSignal recognition particle-docking protein FtsY; 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). (373 aa)    
Predicted Functional Partners:
srp54
Signal recognition particle subunit FFH/SRP54 (srp54); Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Belongs to the GTP-binding SRP family. SRP54 subfamily.
 
0.997
secY
Protein translocase subunit secY/sec61 alpha; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
  
 
 0.963
rpl11
LSU ribosomal protein L11P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors; Belongs to the universal ribosomal protein uL11 family.
 
 
 
 0.945
rpl10
LSU ribosomal protein L10P; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family.
   
 
 0.936
srp19
Signal recognition particle, subunit SRP19 (srp19); Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.
   
 
 0.926
rpl39e
PFAM: ribosomal protein L39e; Belongs to the eukaryotic ribosomal protein eL39 family.
     
 0.904
eif6
Translation initiation factor 6 (aeIF-6); Binds to the 50S ribosomal subunit and prevents its association with the 30S ribosomal subunit to form the 70S initiation complex.
     
 0.902
rpl18a
PFAM: ribosomal LX protein.
  
    0.899
Msed_1625
PFAM: DNA-binding TFAR19-related protein; Belongs to the PDCD5 family.
       0.895
pfdA
Prefoldin, alpha subunit; Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding.
       0.895
Your Current Organism:
Metallosphaera sedula
NCBI taxonomy Id: 399549
Other names: M. sedula DSM 5348, Metallosphaera sedula DSM 5348, Metallosphaera sedula IFO 15509, Metallosphaera sedula JCM 9185, Metallosphaera sedula NBRC 15509, Metallosphaera sedula str. DSM 5348, Metallosphaera sedula strain DSM 5348
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.