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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
fklBPeptidyl-prolyl cis-trans isomerase, FKBP-type, 22 kDa (fklB); Similar to GB:U14003 SP:P39311 PID:537048 GB:U00096 PID:1790652 percent identity: 43.46; identified by sequence similarity; putative. (264 aa)    
Predicted Functional Partners:
ppiB
Peptidyl-prolyl cis-trans isomerase, cyclophilin-binding (cyp); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family.
  
 0.992
htpG
Heat shock protein 90 (htpG); Molecular chaperone. Has ATPase activity.
   
 0.947
dnaK
Heat shock protein 70 (dnaK); Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.921
tp92
Outer membrane protein; Might be part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane; Belongs to the BamA family.
   
 
 0.874
infA
Translation initiation factor 1 (infA); 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.
   
   0.842
rplE
Ribosomal protein L5 (rplE); This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
   
   0.729
rplW
Ribosomal protein L23 (rplW); One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome; Belongs to the universal ribosomal protein uL23 family.
   
 
 0.726
rplR
Ribosomal protein L18 (rplR); This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
   
   0.714
rpoB
DNA-directed RNA polymerase, beta subunit (rpoB); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
  
 0.711
rpmC
Ribosomal protein L29 (rpmC); Similar to SP:P04457 percent identity: 30.36; identified by sequence similarity; putative; Belongs to the universal ribosomal protein uL29 family.
   
   0.705
Your Current Organism:
Treponema pallidum
NCBI taxonomy Id: 243276
Other names: T. pallidum subsp. pallidum str. Nichols, Treponema pallidum Nichols, Treponema pallidum subsp. pallidum str. Nichols
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.