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
ffhSignal recognition particle protein; 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. (456 aa)    
Predicted Functional Partners:
ftsY
Signal 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).
 
0.977
secE
Preprotein translocase, SecE subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
   
 0.916
rpsE
Ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family.
  
 
 0.915
rplD
50S ribosomal protein L4; Forms part of the polypeptide exit tunnel.
  
 0.914
secY
Preprotein translocase, SecY subunit; 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.
    
 0.910
KXB74220.1
Preprotein translocase, SecG subunit; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family.
    
 0.909
rplO
Ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
   
 
 0.908
rplC
50S ribosomal protein L3; 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.
   
 
 0.907
rplM
Ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
  
 
 0.906
rplW
Ribosomal protein L23; One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome; Belongs to the universal ribosomal protein uL23 family.
   
 0.905
Your Current Organism:
Prevotella amnii
NCBI taxonomy Id: 419005
Other names: CCUG 53648, DSM 23384, JCM 14753, P. amnii, Prevotella amnii Lawson et al. 2008 emend. Hahnke et al. 2016
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