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
secYsecY protein; 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. (410 aa)    
Predicted Functional Partners:
secE
Hypothetical protein; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
  
 0.999
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.
 
 
 0.999
KRL61370.1
Hypothetical protein; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family.
   
 0.999
rplN
rplN protein; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family.
 
 
 0.999
rplX
rplX protein; One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
 
 
 0.999
rplE
rplE protein; 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.
 
 
 0.999
KRL58993.1
30S ribosomal protein S8; Belongs to the universal ribosomal protein uS8 family.
 
 
 0.999
rplR
Ribosomal protein L18; 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.
 
 
 0.999
rpsE
rpsE protein; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family.
 0.999
rplO
Ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
 
 
 0.999
Your Current Organism:
Lactobacillus fuchuensis
NCBI taxonomy Id: 1423747
Other names: L. fuchuensis DSM 14340 = JCM 11249, Lactobacillus fuchuensis DSM 14340, Lactobacillus fuchuensis DSM 14340 = JCM 11249, Lactobacillus fuchuensis JCM 11249, Lactobacillus fuchuensis JCM 11249 = DSM 14340
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.