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
cshARNA helicase; DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity; Belongs to the DEAD box helicase family. CshA subfamily. (511 aa)    
Predicted Functional Partners:
AOW73903.1
Recombinase RecQ; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
0.938
AOW75264.1
ATP-dependent DNA helicase RecQ; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
0.931
rplC
50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family.
   
 
 0.754
rplD
50S ribosomal protein L4; Forms part of the polypeptide exit tunnel.
  
 0.729
AOW74894.1
Peptidylprolyl 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.
 
 0.727
dnaJ
Molecular chaperone 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 between DnaJ, [...]
  
 
 0.716
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.
  
 0.697
rplM
50S ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
  
 0.674
AOW73621.1
Ribosome biogenesis GTPase YqeH; In Bacillus subtilis this enzyme appears to be involved in 30S ribosomal RNA subunit biogenesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.665
rbgA
Ribosome biogenesis GTPase YlqF; Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity; Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1 subfamily.
  
 0.665
Your Current Organism:
Pediococcus acidilactici
NCBI taxonomy Id: 1254
Other names: BCRC 80335 [[Pediococcus lolii]], CCUG 32235, CIP 103408, DSM 19927 [[Pediococcus lolii]], DSM 20284, JCM 15055 [[Pediococcus lolii]], LMG 11384, LMG:11384, Lactobacillus sp. Lact11, NCFB 2767, NCIMB 12174, P. acidilactici, Pediococcus lindneri, Pediococcus lolii, Pediococcus lolii Doi et al. 2009, strain B213c, strain Back S213C, strain NGRI 0510Q [[Pediococcus lolii]]
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