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
fklBFKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (206 aa)    
Predicted Functional Partners:
ppiB
Peptidyl-prolyl cis-trans isomerase B (rotamase B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
 
 0.849
htpG
Protein refolding molecular co-chaperone Hsp90, Hsp70-dependent; Molecular chaperone. Has ATPase activity.
   
 0.810
fkpB
FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. Substrate specificity investigated with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide' where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln.
  
   
 0.801
ppiC
Peptidyl-prolyl cis-trans isomerase C (rotamase C); PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates; Belongs to the PpiC/parvulin rotamase family.
   
 
 0.721
surA
Peptidyl-prolyl cis-trans isomerase (PPIase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane- associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis.
   
 
 0.695
apaH
Diadenosine tetraphosphatase; Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family.
    
 0.683
infA
Translation initiation factor IF-1; One of the essential components for the initiation of protein synthesis. Binds in the vicinity of the A-site. 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.
   
   0.679
slyD
FKBP-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...]
  
  
 0.673
tig
Peptidyl-prolyl cis/trans isomerase (trigger factor); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates. Binds to nascent polypeptide chains via ribosomal protein L23. Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity. Belongs to the FKBP-type PPIase family. Tig subfamily.
   
  
 0.640
ppiA
Peptidyl-prolyl cis-trans isomerase A (rotamase 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.
 
 0.546
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.