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
KXG91322.1Putative oxygen-independent coproporphyrinogen III oxidase; KEGG: ols:Olsu_0977 1.3e-80 coproporphyrinogen dehydrogenase K02495; Psort location: Cytoplasmic, score: 9.97. (419 aa)    
Predicted Functional Partners:
lepA
GTP-binding protein LepA; 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.
  
 0.885
KXG91321.1
TIM-barrel protein, nifR3 family; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family.
 
    0.845
KXG90987.1
KEGG: ols:Olsu_0499 0. pyruvate ferredoxin/flavodoxin oxidoreductase; K03737 putative pyruvate-flavodoxin oxidoreductase; Psort location: Cytoplasmic, score: 7.50.
  
  
 0.790
KXG91325.1
tRNA methylthiotransferase YqeV; KEGG: cth:Cthe_0150 2.2e-69 RNA modification protein; K08070 2-alkenal reductase; Psort location: Cytoplasmic, score: 7.50.
 
  
 0.710
rlmN
23S rRNA methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family.
 
   
 0.626
KXG91323.1
DnaJ domain protein; KEGG: apb:SAR116_1614 2.3e-28 DnaJ family molecular chaperone K03686; Psort location: Cytoplasmic, score: 9.97.
  
    0.588
dnaJ
Putative chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwee [...]
  
    0.540
KXG91326.1
Putative PhoH-like protein; KEGG: cnc:CNE_1c05490 4.2e-59 phoH; phosphate starvation-inducible protein PhoH K06217; Psort location: Cytoplasmic, score: 9.97.
     
 0.503
rpsT
Ribosomal protein S20; Binds directly to 16S ribosomal RNA.
       0.493
KXG91338.1
Ribosomal protein S12 methylthiotransferase RimO; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily.
 
  
 0.488
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
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.