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
AQR99311.1Subtilase family protein. (618 aa)    
Predicted Functional Partners:
AQR99310.1
Subtilase family protein.
 
    
0.838
AQS01211.1
Putative peptidoglycan binding domain protein.
  
 0.807
AQR98334.1
Hypothetical protein.
 
 
 0.692
spoIIIE
DNA translocase SpoIIIE; Belongs to the FtsK/SpoIIIE/SftA family.
  
 
 0.633
ssb
Single-stranded DNA-binding protein.
  
     0.626
AQR99740.1
Hypothetical protein.
  
 
 0.612
AQS00406.1
Hypothetical protein.
  
 
 0.612
lytA_19
Autolysin.
  
 
 0.612
AQS02397.1
Hypothetical protein.
  
 
 0.612
secY
Protein 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.
    
 
 0.595
Your Current Organism:
Clostridium saccharobutylicum
NCBI taxonomy Id: 169679
Other names: ATCC BAA-117, C. saccharobutylicum, Clostridium saccharobutylicum Keis et al. 2001, DSM 13864, strain NCP 262
Server load: medium (52%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.