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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
secYPreprotein translocase; 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. Complements an E.coli temp [...] (468 aa)    
Predicted Functional Partners:
secE
Protein transport protein sec61 gamma subunit; Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation; Belongs to the SecE/SEC61-gamma family.
   
 
 0.995
rpl32e
Function Code: 13.4 Translation: Ribosomal proteins: synthesis and modification; (rpl32E).
 
  
 0.945
rpl30
Function Code: 13.4 Translation: Ribosomal proteins: synthesis and modification; (rpl30P).
 
    0.939
ftsY
Signal recognition particle receptor (dpa); 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).
    
 0.928
rps5
SSU ribosomal protein S5P; With S4 and S12 plays an important role in translational accuracy.
 
  
 0.926
rpl19e
LSU ribosomal protein L19E; Binds to the 23S rRNA; Belongs to the eukaryotic ribosomal protein eL19 family.
 
    0.924
rpl15
LSU ribosomal protein L15P; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
 
  
 0.920
srp54
Signal recognition particle protein 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.
     
 0.917
rpl6
LSU ribosomal protein L6P; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
 
  
 0.917
rpl4
LSU ribosomal protein L4P; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
 
    0.912
Your Current Organism:
Pyrococcus furiosus
NCBI taxonomy Id: 186497
Other names: P. furiosus DSM 3638, Pyrococcus furiosus DSM 3638, Pyrococcus furiosus str. DSM 3638, Pyrococcus furiosus strain DSM 3638
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.