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
SEC90008.1Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); 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. (167 aa)    
Predicted Functional Partners:
nuoC
NADH dehydrogenase subunit C /NADH dehydrogenase subunit 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.
   
 
 0.999
SEC55311.1
Acyl transferase domain-containing protein.
  
 
 0.989
SEC07169.1
Non-ribosomal peptide synthase domain TIGR01720/amino acid adenylation domain-containing protein.
  
 
 0.984
fusA
Translation elongation factor 2 (EF-2/EF-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. [...]
   
 0.926
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, [...]
 
 
 0.924
SED56839.1
Curved DNA-binding protein.
 
 
 0.924
rplU
LSU ribosomal protein L21P; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
  
   0.915
rpsQ
SSU ribosomal protein S17P; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
   
   0.912
rplO
LSU ribosomal protein L15P; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
   
 
 0.912
rplK
LSU ribosomal protein L11P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
   
   0.910
Your Current Organism:
Pseudomonas taetrolens
NCBI taxonomy Id: 47884
Other names: ATCC 4683, CCUG 560, CFBP 5592, CIP 103299, JCM 20238, LMG 2336, LMG:2336, NCIB 9396, NCIB:9396, NCTC 10697, NRRL B-14, NRRL B-731, NRRL:B:14, NRRL:B:731, P. taetrolens, VKM B-904, VKM:B:904
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