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
ERK55586.1Preprotein translocase, YajC subunit; KEGG: apb:SAR116_0407 1.9e-08 YajC K03210. (88 aa)    
Predicted Functional Partners:
secD
Export membrane protein SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
  
 
 0.836
secF
Export membrane protein SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
  
 
 0.791
ERK52864.1
Preprotein translocase, SecE subunit; Belongs to the SecE/SEC61-gamma family.
   
 
 0.764
ERK47704.1
KEGG: apb:SAR116_1635 0.00021 protein-export protein SecB K03071; Psort location: Cytoplasmic, score: 8.96.
   
 
 0.723
secY
Preprotein translocase, SecY subunit; 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.
   
 
 0.702
ERK55585.1
KEGG: lba:Lebu_0296 3.3e-153 N-acetylmuramoyl-L-alanine amidase; K01448 N-acetylmuramoyl-L-alanine amidase; Psort location: Extracellular, score: 9.65.
       0.679
ftsY
Signal recognition particle-docking protein FtsY; 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).
    
 0.657
ERK51990.1
Stage III sporulation protein J family protein; Psort location: CytoplasmicMembrane, score: 10.00.
   
 
 0.656
ffh
Signal 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.
    
 0.655
secA
Preprotein translocase, SecA subunit; 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.
     
 0.650
Your Current Organism:
Leptotrichia sp. F0557
NCBI taxonomy Id: 1227268
Other names: L. sp. oral taxon 879 str. F0557, Leptotrichia sp. oral taxon 879 str. F0557
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.