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
srp54Signal 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. (433 aa)    
Predicted Functional Partners:
Pisl_0461
KEGG: pai:PAE3100 signal recognition particle protein (docking protein), probable; TIGRFAM: signal recognition particle-docking protein FtsY; PFAM: GTP-binding signal recognition particle SRP54, G- domain; GTP-binding signal recognition particle SRP54, helical bundle; SMART: AAA ATPase.
 
0.999
rpl24
LSU ribosomal protein L24P; One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
  
 0.999
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.
   
 0.999
rpl29
PFAM: ribosomal protein L29; KEGG: pai:PAE1778 ribosomal protein L29; Belongs to the universal ribosomal protein uL29 family.
  
 
 0.999
rpl22
LSU ribosomal protein L22P; This protein binds specifically to 23S rRNA. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
  
 
 0.999
rpl23
LSU ribosomal protein L23P; 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.
  
 0.999
rps9
PFAM: ribosomal protein S9; KEGG: pai:PAE0674 ribosomal protein S9; Belongs to the universal ribosomal protein uS9 family.
 
 0.998
rpl3
LSU 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.
 
 
 0.998
rpl13
LSU ribosomal protein L13P; 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.
  
 
 0.997
rpl2
LSU 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.
  
 
 0.997
Your Current Organism:
Pyrobaculum islandicum
NCBI taxonomy Id: 384616
Other names: P. islandicum DSM 4184, Pyrobaculum islandicum DSM 4184, Pyrobaculum islandicum str. DSM 4184, Pyrobaculum islandicum strain DSM 4184
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.