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
rpmDCOGs: COG1841 Ribosomal protein L30/L7E; InterPro IPR016082:IPR005996; KEGG: bfs:BF3985 50S ribosomal protein L30; PFAM: Ribosomal protein L30, ferredoxin-like fold domain; SPTR: 50S ribosomal protein L30; TIGRFAM: Ribosomal protein L30, bacterial-type; manually curated; PFAM: Ribosomal protein L30p/L7e; TIGRFAM: ribosomal protein L30, bacterial/organelle. (58 aa)    
Predicted Functional Partners:
rplO
Ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
 0.999
rplR
Ribosomal protein L18; 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
rplF
Ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
  
 0.999
rplX
Ribosomal protein L24; One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
  
 0.998
rpmC
Ribosomal protein L29; InterPro IPR001854; KEGG: bvu:BVU_0797 50S ribosomal protein L29; PFAM: Ribosomal protein L29; SPTR: 50S ribosomal protein L29; TIGRFAM: Ribosomal protein L29; PFAM: Ribosomal L29 protein; TIGRFAM: ribosomal protein L29; Belongs to the universal ribosomal protein uL29 family.
  
 0.998
rplV
Ribosomal protein L22; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
  
 0.998
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.
  
 
 0.997
rplW
Ribosomal protein L25/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.
  
 0.997
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.
  
 0.997
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.
  
 0.996
Your Current Organism:
Bacteroides salanitronis
NCBI taxonomy Id: 667015
Other names: B. salanitronis DSM 18170, Bacteroides salanitronis BL78, Bacteroides salanitronis DSM 18170, Bacteroides salanitronis JCM 13657, Bacteroides salanitronis str. DSM 18170, Bacteroides salanitronis strain DSM 18170
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.