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
ARQ06445.1Putative peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (196 aa)    
Predicted Functional Partners:
ARQ06577.1
Putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern.
 
    0.888
menE
2-succinylbenzoate--CoA ligase; Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA); Belongs to the ATP-dependent AMP-binding enzyme family. MenE subfamily.
  
 
 0.873
fusA
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 subfamily.
   
 0.832
rplU
50S ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
  
   0.827
rpsQ
30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
   
   0.822
rplO
50S ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
   
   0.816
rplQ
50S ribosomal protein L17; Bacteria and source DNA available from Institute of Veterinary Bacteriology, University Bern.
   
   0.815
rplX
50S ribosomal protein L24; One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
   
   0.813
rplK
50S ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
   
   0.809
rsfS
Ribosomal silencing factor RsfS; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
  
   0.787
Your Current Organism:
Macrococcus canis
NCBI taxonomy Id: 1855823
Other names: CCM 8748, CCOS 969, CCOS:969, CCUG 68920, DSM 101690, M. canis, Macrococcus canis Gobeli Brawand et al. 2017, Macrococcus sp. KM45013, strain KM 45013
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