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
rpsLSSU 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. (123 aa)    
Predicted Functional Partners:
rpsR
SSU ribosomal protein S18P; Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit; Belongs to the bacterial ribosomal protein bS18 family.
  
 0.999
rpsF
SSU ribosomal protein S6P; Binds together with S18 to 16S ribosomal RNA.
  
 0.999
rpsU
SSU ribosomal protein S21P; Belongs to the bacterial ribosomal protein bS21 family.
   
 0.999
rplK
LSU ribosomal protein L11P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
 
 
 0.999
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.
 
 0.999
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
rplL
LSU ribosomal protein L12P; 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.
 
 
 0.999
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.
 0.999
fusA
Translation elongation factor 2 (EF-2/EF-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. [...]
 0.999
tuf
Translation elongation factor 1A (EF-1A/EF-Tu); This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.
 
 0.999
Your Current Organism:
Pseudomonas psychrophila
NCBI taxonomy Id: 122355
Other names: CCUG 53877, CIP 107901, DSM 17535, JCM 10889, P. psychrophila, Pseudomonas psychrophila Yumoto et al. 2002, Pseudomonas sp. CF149, Pseudomonas sp. E-3, strain E-3
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