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
APV41303.1Peptidylprolyl isomerase A; 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. (185 aa)    
Predicted Functional Partners:
htpG
Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.
 
 0.885
nuoC
NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
   
 
 0.871
APV41304.1
3-oxoadipate enol-lactonase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.828
APV41305.1
LysR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the LysR transcriptional regulatory family.
  
    0.761
APV41311.1
RNA helicase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the DEAD box helicase family.
 
 0.707
fusA
Translation 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 s [...]
   
 0.706
rhlE
DEAD/DEAH box helicase; DEAD-box RNA helicase involved in ribosome assembly. Has RNA- dependent ATPase activity and unwinds double-stranded RNA.
 
 0.693
APV40622.1
DEAD/DEAH box helicase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the DEAD box helicase family.
 
 0.693
APV39334.1
DNA-binding protein; Functional analog of DnaJ; co-chaperone with DnaK, molecular chaperone in an adaptive response to environmental stresses other than heat shock; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.690
rhlB
ATP-dependent RNA helicase RhlB; DEAD-box RNA helicase involved in RNA degradation. Has RNA- dependent ATPase activity and unwinds double-stranded RNA. Belongs to the DEAD box helicase family. RhlB subfamily.
 
 0.684
Your Current Organism:
Pseudomonas frederiksbergensis
NCBI taxonomy Id: 104087
Other names: ATCC BAA-257, CIP 106887, DSM 13022, LMG 19851, LMG:19851, P. frederiksbergensis, Pseudomonas frederiksbergensis Andersen et al. 2000, Pseudomonas sp. BDR1P1B1, Pseudomonas sp. BDR1P1B2, Pseudomonas sp. V1D5a, strain JAJ28
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