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
rnyRibonuclease Y; Endoribonuclease that initiates mRNA decay. (509 aa)    
Predicted Functional Partners:
PSM36_0708
Cell fate regulator YaaT, PSP1 superfamily (controls sporulation, competence, biofilm development) [Signal transduction mechanisms]; High confidence in function and specificity.
 
  
 0.843
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
  
 
 0.668
PSM36_1650
Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]; High confidence in function and specificity.
  
 
 0.641
pfkA1
6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis; Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.
  
 
 0.629
pfkA3
6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
  
 
 0.629
pfp
Diphosphate-fructose-6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
  
 
 0.629
PSM36_1624
Hypothetical protein; High confidence in function and specificity.
   
 
 0.607
PSM36_0001
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; High confidence in function and specificity; Belongs to the DEAD box helicase family.
   
 
 0.593
PSM36_0716
Superfamily II DNA and RNA helicase; High confidence in function and specificity; Belongs to the DEAD box helicase family.
   
 
 0.593
rhlE
DEAD-box RNA helicase involved in ribosome assembly. Has RNA-dependent ATPase activity and unwinds double-stranded RNA. May play a role in the interconversion of ribosomal RNA-folding intermediates that are further processed by DeaD or SrmB during ribosome maturation; High confidence in function and specificity.
   
 
 0.593
Your Current Organism:
Proteiniphilum saccharofermentans
NCBI taxonomy Id: 1642647
Other names: CECT 8610, DSM 28694, LMG 28299, LMG:28299, P. saccharofermentans, Proteiniphilum saccharofermentans Hahnke et al. 2016, Proteiniphilum sp. M3/6, strain M3/6
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.