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
ffhSignal recognition particle protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Belongs to the GTP-binding SRP family. SRP54 subfamily. (493 aa)    
Predicted Functional Partners:
ftsY
Cell division protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
 
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.
    
 0.978
secE
Protein translocase subunit SecE; Belongs to the SecE/SEC61-gamma family.
   
 0.974
LRC_12040
Signal recognition particle associated protein; Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein.
  
  
 0.972
secG
Protein translocase subunit SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family.
    
 0.970
rpsP
30S ribosomal protein S16; Belongs to the bacterial ribosomal protein bS16 family.
 
 
 0.952
yidC
Stage III sporulation protein J; 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; Belongs to the OXA1/ALB3/YidC family. Type 2 subfamily.
   
 0.952
LRC_10530
Preprotein translocase subunit YidC.
   
 0.948
secA
Protein translocase subunit SecA; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
    
 0.946
yajC
Preprotein translocase subunit.
    
 0.927
Your Current Organism:
Lactobacillus ruminis
NCBI taxonomy Id: 1069534
Other names: L. ruminis ATCC 27782, Lactobacillus ruminis ATCC 27782, Lactobacillus ruminis str. ATCC 27782, Lactobacillus ruminis strain ATCC 27782
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.