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
rplARibosomal protein L1 (rplA); Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release. (226 aa)    
Predicted Functional Partners:
infA
Translation initiation factor 1 (infA); One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
  
 
 0.999
rplD
Ribosomal protein L4 (rplD); 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.
  
 0.999
rplW
Ribosomal protein L23 (rplW); 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.
  
 0.999
rplV
Ribosomal protein L22 (rplV); This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. 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 (By similarity).
  
 0.999
rpmC
Ribosomal protein L29 (rpmC); Similar to SP:P04457 percent identity: 30.36; identified by sequence similarity; putative; Belongs to the universal ribosomal protein uL29 family.
  
 0.999
rplX
Ribosomal protein L24 (rplX); 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
rplR
Ribosomal protein L18 (rplR); 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.
  
 0.999
rplK
Ribosomal protein L11 (rplK); Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
 
 0.999
rplJ
Ribosomal protein L10 (rplJ); 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.
 
 0.999
gltX
glutamyl-tRNA synthetase (gltX); Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
  
 0.999
Your Current Organism:
Treponema pallidum
NCBI taxonomy Id: 243276
Other names: T. pallidum subsp. pallidum str. Nichols, Treponema pallidum Nichols, Treponema pallidum subsp. pallidum str. Nichols
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.