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
rplLLSU ribosomal protein L7/L12; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family. (121 aa)    
Predicted Functional Partners:
rplJ
LSU ribosomal protein L10p; 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
rplK
LSU ribosomal protein L11p; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
 
 
 0.996
rplA
LSU ribosomal protein L1p; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
 
 
 0.995
fusA
Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]
 
 
 0.993
rpsG
SSU ribosomal protein S7p; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.
 
 
 0.992
rplM
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.
 
 
 0.992
rpsL
SSU ribosomal protein S12p; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
 
 
 0.991
rpsB
SSU ribosomal protein S2p Sae; Belongs to the universal ribosomal protein uS2 family.
 
 
 0.991
rpmA
LSU ribosomal protein L27p; Belongs to the bacterial ribosomal protein bL27 family.
 
 
 0.991
rplX
LSU ribosomal protein L24p; One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
 
 
 0.990
Your Current Organism:
Bacillus smithii
NCBI taxonomy Id: 1479
Other names: B. smithii, CCUG 27413, CIP 103790, DSM 4216, IFO 15311, JCM 9076, LMG 12526, LMG:12526, NBRC 15311, NRRL NRS-173
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.