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
lepB1Signal peptidase I; Belongs to the peptidase S26 family. (262 aa)    
Predicted Functional Partners:
lepB2
Signal peptidase I; Belongs to the peptidase S26 family.
 
  
0.983
rnhB
Ribonuclease HII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
  
  
 0.920
lepA
GTP-binding elongation factor; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
  
 
 0.844
phoU
Phosphate uptake regulator.
  
    0.704
alaS
Alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
  
  
 0.699
tpx
Thiol peroxidase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. Tpx subfamily.
   
    0.697
ACP32767.1
Hypothetical protein; Predicted nucleoside-diphosphate sugar epimerase.
   
    0.694
tuf
Elongation factor EF-Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.
   
  
 0.673
gyrA
DNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
  
  
 0.637
rplS
50S ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
  
    0.626
Your Current Organism:
Corynebacterium aurimucosum
NCBI taxonomy Id: 548476
Other names: C. aurimucosum ATCC 700975, Corynebacterium aurimucosum ATCC 700975, Corynebacterium aurimucosum CCUG 48176, Corynebacterium aurimucosum CIP 107436, Corynebacterium aurimucosum CN-1, Corynebacterium aurimucosum DSM 44827, Corynebacterium aurimucosum str. ATCC 700975, Corynebacterium aurimucosum strain ATCC 700975, Corynebacterium nigricans CN-1
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.