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
SDE03778.1GTPase, G3E family. (366 aa)    
Predicted Functional Partners:
rpmB
Large subunit ribosomal protein L28; Belongs to the bacterial ribosomal protein bL28 family.
 
  
 0.938
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.
  
 
 0.895
rpmF
Large subunit ribosomal protein L32; Belongs to the bacterial ribosomal protein bL32 family.
 
    0.891
rpmJ-2
LSU ribosomal protein L36P; Belongs to the bacterial ribosomal protein bL36 family.
 
  
 0.852
SDE61547.1
Zinc transport system substrate-binding protein; Belongs to the bacterial solute-binding protein 9 family.
  
  
 0.816
rpmE2
Large subunit ribosomal protein L31.
  
  
 0.790
rpmG
LSU ribosomal protein L33P; Belongs to the bacterial ribosomal protein bL33 family.
 
  
 0.717
map-3
Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
  
 
   0.711
map
Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
  
 
   0.697
map-2
Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
    
   0.657
Your Current Organism:
Auraticoccus monumenti
NCBI taxonomy Id: 675864
Other names: A. monumenti, Auraticoccus monumenti Alonso-Vega et al. 2011, CECT 7672, DSM 23257, LMG 25551, LMG:25551, Propionibacteriaceae bacterium MON 2.2, strain MON 2.2
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.