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
EIC31190.1Hypothetical protein. (686 aa)    
Predicted Functional Partners:
htpG
Molecular chaperone of HSP90 family; Molecular chaperone. Has ATPase activity.
   
 0.995
grpE
Molecular chaperone GrpE (heat shock protein); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...]
  
 0.981
EIC29258.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain.
   
 0.960
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]
   
 0.960
EIC30823.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
   
 0.960
rplP
Ribosomal protein L16, bacterial/organelle; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family.
   
 0.930
EIC28996.1
PFAM: NifU-like N terminal domain; TIGRFAM: SUF system FeS assembly protein, NifU family.
  
 
 0.918
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.909
EIC27989.1
PFAM: von Willebrand factor type A domain; Tetratricopeptide repeat.
    
 0.881
EIC28812.1
Hypothetical protein; PFAM: Plant specific mitochondrial import receptor subunit TOM20.
    
 0.881
Your Current Organism:
Methylomicrobium album
NCBI taxonomy Id: 686340
Other names: M. album BG8, Methylomicrobium album BG8, Methylomicrobium album str. BG8, Methylomicrobium album strain BG8
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.