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
glySKEGG: ols:Olsu_0881 2.2e-211 glycyl-tRNA synthetase subunit beta K01879; Psort location: Cytoplasmic, score: 9.97. (698 aa)    
Predicted Functional Partners:
glyQ
glycine--tRNA ligase, alpha subunit; KEGG: apv:Apar_0693 2.9e-138 glyQ; glycyl-tRNA synthetase subunit alpha K01878; Psort location: Cytoplasmic, score: 9.97.
 0.999
KXG89141.1
Hypothetical protein; Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
  
    0.847
trmD
tRNA (guanine-N(1)-)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family.
  
  
 0.787
ileS
isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.
 
  
 0.712
valS
valine--tRNA ligase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
  
  
 0.689
KXG89138.1
KEGG: ols:Olsu_0879 2.7e-48 signal peptidase I K03100; Psort location: CytoplasmicMembrane, score: 8.78; Belongs to the peptidase S26 family.
       0.660
rpsP
Ribosomal protein S16; KEGG: apb:SAR116_1817 2.0e-20 30S ribosomal protein S16 K02959; Psort location: Cytoplasmic, score: 9.97; Belongs to the bacterial ribosomal protein bS16 family.
  
    0.656
leuS
leucine--tRNA ligase; KEGG: ols:Olsu_1022 0. leucyl-tRNA synthetase K01869; Psort location: Cytoplasmic, score: 9.97; Belongs to the class-I aminoacyl-tRNA synthetase family.
   
  
 0.648
KXG89135.1
Hypothetical protein; KEGG: swi:Swit_1461 0.0011 1-deoxy-D-xylulose-5-phosphate synthase K01662; Psort location: Cytoplasmic, score: 7.50; Belongs to the UPF0109 family.
       0.647
KXG89136.1
Hypothetical protein; An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
       0.647
Your Current Organism:
Atopobium vaginae
NCBI taxonomy Id: 82135
Other names: A. vaginae, ATCC BAA-55, ATCC:BAA 55, ATCC:BAA:55, CCUG 38953, CIP 106431, DSM 15829, NCTC 13935
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.