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
rpsICOGs: COG0103 Ribosomal protein S9; InterPro IPR000754:IPR017441:IPR020574; KEGG: mlo:mll8456 30S ribosomal protein S9; PFAM: ribosomal protein S9; SPTR: 30S ribosomal protein S9; PFAM: Ribosomal protein S9/S16; Belongs to the universal ribosomal protein uS9 family. (160 aa)    
Predicted Functional Partners:
rpsO
Ribosomal protein S15; Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
 
 0.999
rpsP
COGs: COG0228 Ribosomal protein S16; InterPro IPR000307; KEGG: mlo:mlr4381 30S ribosomal protein S16; PFAM: ribosomal protein S16; SPTR: Ribosomal protein S16; TIGRFAM: ribosomal protein S16; PFAM: Ribosomal protein S16; TIGRFAM: ribosomal protein S16; Belongs to the bacterial ribosomal protein bS16 family.
 
 0.999
rplU
Ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
 
 
 0.999
rpmA
COGs: COG0211 Ribosomal protein L27; InterPro IPR001684:IPR018261; KEGG: mlo:msl4017 50S ribosomal protein L27; PFAM: ribosomal protein L27; SPTR: Ribosomal protein L27; TIGRFAM: ribosomal protein L27; PFAM: Ribosomal L27 protein; TIGRFAM: ribosomal protein L27; Belongs to the bacterial ribosomal protein bL27 family.
 
 
 0.999
rpsB
COGs: COG0052 Ribosomal protein S2; InterPro IPR005706:IPR001865:IPR018130; KEGG: mlo:mll0651 30S ribosomal protein S2; PFAM: ribosomal protein S2; SPTR: Ribosomal protein S2; TIGRFAM: ribosomal protein S2; PFAM: Ribosomal protein S2; TIGRFAM: ribosomal protein S2, bacterial type; Belongs to the universal ribosomal protein uS2 family.
 
 0.999
rplQ
COGs: COG0203 Ribosomal protein L17; InterPro IPR000456; KEGG: mlo:mlr0326 50S ribosomal protein L17; PFAM: ribosomal protein L17; SPTR: 50S ribosomal protein L17; TIGRFAM: ribosomal protein L17; PFAM: Ribosomal protein L17; TIGRFAM: ribosomal protein L17.
 
 
 0.999
rpsK
30S ribosomal protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family.
 
 0.999
rplO
Ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
 
 
 0.999
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.
 
 0.999
rpsH
Ribosomal protein S8; One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit; Belongs to the universal ribosomal protein uS8 family.
 
 
 0.999
Your Current Organism:
Mesorhizobium opportunistum
NCBI taxonomy Id: 536019
Other names: M. opportunistum WSM2075, Mesorhizobium opportunistum WSM2075, Mesorhizobium opportunistum str. WSM2075, Mesorhizobium opportunistum strain WSM2075, Mesorhizobium sp. LMG 24607, Mesorhizobium sp. WSM2075
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.