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
secEPreprotein translocase, SecE subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. (161 aa)    
Predicted Functional Partners:
secG
Protein-export membrane protein secG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family.
 
 0.999
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.
  
 0.998
secA-2
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; Belongs to the SecA family.
    
 0.993
rplK
50S ribosomal subunit protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
  
 
 0.990
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.
  
 0.988
ftsY
Cell division protein ftsY homolog; 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).
    
 0.986
nusG
Transcription antitermination protein nusG; Participates in transcription elongation, termination and antitermination.
  
  
 0.984
CCH88769.1
Preprotein translocase; Function of strongly homologous gene; transporter.
  
 
 0.983
oxaA
Preprotein translocase subunit YidC; Function of homologous gene experimentally demonstrated in an other organism; cell process.
   
 0.977
rplA
50S ribosomal subunit protein L1; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
  
 
 0.976
Your Current Organism:
Modestobacter marinus
NCBI taxonomy Id: 477641
Other names: CGMCC 4.5581, DSM 45201, M. marinus, Modestobacter marinus Xiao et al. 2011, Modestobacter sp. 42H12-1, strain 42H12-1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.