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
ftsYCell division 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). (396 aa)    
Predicted Functional Partners:
ffh
Signal recognition particle; 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.
 
0.995
ALT35890.1
Preprotein translocase subunit SecY; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SecY/SEC61-alpha family.
   
 0.930
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.
   
 
 0.930
rplW
50S 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.
   
 
 0.925
ALT35899.1
50S ribosomal protein L18; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.923
ALT35912.1
50S ribosomal protein L2; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.922
rplO
50S ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
 
 0.921
rplE
50S ribosomal protein L5; This is 1 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. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
  
 
 
 0.913
rpmC
50S ribosomal protein L29; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uL29 family.
  
 
 
 0.912
rplM
50S 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.
  
 
 0.909
Your Current Organism:
Cutibacterium acnes
NCBI taxonomy Id: 1747
Other names: ATCC 6919, Bacillus acnes, C. acnes, CIP 53.117, Corynebacterium acnes, DSM 16379, JCM 6425, LMG 16711, LMG:16711, NCTC 737, NRRL B-4224, Propionibacterium acnes, Propionicibacterium acnes
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.