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
ftsYSignal recognition particle GTPase; 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). (301 aa)    
Predicted Functional Partners:
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.
 
0.999
secY
Preprotein translocase subunit SecY; 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.
    
 0.936
rpl15
50S ribosomal protein L15P; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
 
 
 0.896
CL1_1444
Signal recognition particle protein SRP19; COG1400.
   
 
 0.862
rps9
30S ribosomal protein S9; COG0103; Belongs to the universal ribosomal protein uS9 family.
 
 
 0.859
rpl3
50S ribosomal protein L3P; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family.
 
 
 0.859
rpl23
50S ribosomal protein L23; Binds to 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Belongs to the universal ribosomal protein uL23 family.
  
 
 0.834
rpl18
50S ribosomal protein L18P; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
   
 
 0.828
rpl2
50S ribosomal protein L2P; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
  
 
 0.825
rpl10
Acidic ribosomal protein P0/50S ribosomal protein L10; 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.
   
 
 0.818
Your Current Organism:
Thermococcus cleftensis
NCBI taxonomy Id: 163003
Other names: DSM 27260, KACC 17922, T. cleftensis, Thermococcus cleftensis Hensley et al. 2014, Thermococcus sp. CL1, strain CL1
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