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
ftsYFused signal recognition particle receptor; 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). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components. (456 aa)    
Predicted Functional Partners:
ffh
Signal recognition particle subunit FFH/SRP54 (srp54); 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. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the i [...]
 
0.999
secY
Protein translocase subunit secY/sec61 alpha; 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
secE
Protein translocase subunit secE/sec61 gamma; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation; Belongs to the SecE/SEC61-gamma family.
    
 0.994
SDT40875.1
Protein translocase subunit secG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family.
   
 0.991
rplO
LSU ribosomal protein L15P; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
 
 
 0.982
rplC
LSU ribosomal protein L3P; 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.
   
 
 0.978
rplW
LSU ribosomal protein L23P.
   
 
 0.977
rplR
LSU ribosomal protein L18P; 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.
   
 
 0.976
SDT47344.1
LSU ribosomal protein L2P.
   
 
 0.975
rplD
LSU ribosomal protein L4P; Forms part of the polypeptide exit tunnel.
  
 
 0.974
Your Current Organism:
Pseudomonas cedrina
NCBI taxonomy Id: 651740
Other names: CFML 96-198, CIP 105541, DSM 17516, P. cedrina, Pseudomonas cedrella, Pseudomonas cedrina corrig. Dabboussi et al. 2002 emend. Behrendt et al. 2009, Pseudomonas sp. H-R, Pseudomonas sp. HG-K2, Pseudomonas sp. LB-C, Pseudomonas sp. LB-Z10, Pseudomonas sp. LB-Z3
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