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
rsgARibosome biogenesis GTPase; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit; Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA subfamily. (344 aa)    
Predicted Functional Partners:
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.
   
   0.935
rpsM
SSU ribosomal protein S13P; Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. Belongs to the universal ribosomal protein uS13 family.
    
   0.927
rpsI
SSU ribosomal protein S9P; Belongs to the universal ribosomal protein uS9 family.
    
   0.925
rpsO
SSU ribosomal protein S15P; Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
  
   0.918
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.
   
   0.917
rpsU
SSU ribosomal protein S21P; Belongs to the bacterial ribosomal protein bS21 family.
   
   0.907
rpsP
SSU ribosomal protein S16P; Belongs to the bacterial ribosomal protein bS16 family.
    
   0.906
rpsN
SSU ribosomal protein S14P; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family.
    
   0.906
rpsC
SSU ribosomal protein S3P; Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation; Belongs to the universal ribosomal protein uS3 family.
    
   0.906
rpsJ
SSU ribosomal protein S10P; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family.
    
   0.906
Your Current Organism:
Tropicimonas isoalkanivorans
NCBI taxonomy Id: 441112
Other names: DSM 19548, JCM 14837, T. isoalkanivorans, Tropicimonas isoalkanivorans Harwati et al. 2009, alpha proteobacterium B51, strain B51
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.