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
ftsYCell division protein (ftsY); Similar to SP:P51835 percent identity: 38.16; identified by sequence similarity; putative. (295 aa)    
Predicted Functional Partners:
ffh
Signal recognition particle protein (ffh); Similar to GB:AE000783 percent identity: 45.01; identified by sequence similarity; putative.
 
0.999
secY
Preprotein translocase subunit (secY); The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
   
 0.997
secG
Predicted coding region TP0536; Involved in protein export. Participates in an early event of protein translocation (By similarity); Belongs to the SecG family.
   
 0.994
secE
Preprotein translocase subunit (secE); Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
    
 0.993
rplO
Ribosomal protein L15 (rplO); Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
 
 0.964
yidC
Membrane protein; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
   
 
 0.962
rplC
Ribosomal protein L3 (rplC); One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family.
   
 
 0.959
rplK
Ribosomal protein L11 (rplK); Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
   
 
 0.958
rplJ
Ribosomal protein L10 (rplJ); Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family.
   
 
 0.957
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.
   
 
 0.955
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.