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
TP_0098Heat-shock protein, putative; Similar to PID:1046215 SP:P50025 percent identity: 45.69; identified by sequence similarity; putative. (216 aa)    
Predicted Functional Partners:
dnaK
Heat shock protein 70 (dnaK); Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.999
htpG
Heat shock protein 90 (htpG); Molecular chaperone. Has ATPase activity.
  
 0.996
TP_0100
Thioredoxin, putative; Similar to GB:Z23140 SP:P43221 PID:312981 percent identity: 33.05; identified by sequence similarity; putative.
   
 0.982
grpE
grpE protein (grpE); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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-depe [...]
 
 
 0.977
rpsG
Ribosomal protein S7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.
   
 
 0.944
spoU2
rRNA methylase, putative; Similar to GB:D26185 SP:Q06753 GB:L14580 PID:467483 PID:532360 percent identity: 37.93; identified by sequence similarity; putative; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
   
   0.942
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.
  
 
 0.942
mnmE
Thiophene and furan oxidation protein (thdF); Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
   
 
 0.940
rplQ
Ribosomal protein L17 (rplQ); Similar to GB:AE000783 percent identity: 59.02; identified by sequence similarity; putative.
  
   0.939
rplB
Ribosomal protein L2 (rplB); One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
   
 
 0.938
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.