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
EEF63255.1PFAM: peptidylprolyl isomerase FKBP-type; KEGG: bac:BamMC406_3736 peptidylprolyl isomerase FKBP-type. (110 aa)    
Predicted Functional Partners:
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
 0.958
EEF59832.1
Peptidyl-prolyl cis-trans isomerase cyclophilin type; 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.
 
  
  0.933
EEF59833.1
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.
 
  
  0.933
EEF58233.1
Hypothetical protein; KEGG: rba:RB1912 signal peptide.
    
 0.794
dinB-2
DNA-directed DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
    
   0.779
EEF62702.1
Aspartate kinase; KEGG: min:Minf_2090 aspartokinase; TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; Belongs to the aspartokinase family.
    
   0.655
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...]
    
  0.577
EEF63256.1
KEGG: pap:PSPA7_4357 hypothetical protein.
       0.572
EEF58170.1
Translation initiation factor IF-1; One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
   
   0.488
infA
Translation initiation factor IF-1; One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
   
   0.488
Your Current Organism:
Pedosphaera parvula
NCBI taxonomy Id: 320771
Other names: P. parvula Ellin514, Pedosphaera parvula Ellin514, Pedosphaera parvula str. Ellin514, Pedosphaera parvula strain Ellin514, bacterium Ellin514
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.