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:
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Gene Fusion
Cooccurrence
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[Homology]
Score
grpEProtein grpE; 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. Several rounds of ATP-dependent i [...] (178 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein dnaK; Acts as a chaperone.
 
 
 0.999
ADZ09712.1
Heat shock protein DnaJ domain protein; KEGG: pfh:PFHG_00645 hypothetical protein similar to chaperone protein J; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal.
 
 
 0.997
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 [...]
 
 
 0.994
ADZ09610.1
Thermosome; KEGG: mmg:MTBMA_c06670 thermosome, subunit alpha (chaperonin subunit); TIGRFAM: Thermosome, archaeal; PFAM: Chaperonin Cpn60/TCP-1.
 
 0.971
ADZ10121.1
Thermosome; KEGG: mth:MTH794 chaperonin; TIGRFAM: Thermosome, archaeal; PFAM: Chaperonin Cpn60/TCP-1.
 
 0.970
ADZ09250.1
Peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
  
 
 0.695
dnaG
UPF0095 protein; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteropolymeric, adenine-rich transcripts and the exosome.
  
  
 0.690
uvrC
UvrABC system protein C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
 
   
 0.651
ADZ09740.1
TIGRFAM: Peptidase S16, archaeal lon homologues; PFAM: Peptidase S16, Lon C-terminal; ATPase, AAA-5; KEGG: mth:MTH785 ATP-dependent protease Lon; SMART: ATPase, AAA+ type, core; Belongs to the peptidase S16 family.
  
  
 0.650
ADZ10420.1
TIGRFAM: Peptidase S16, archaeal lon homologues; PFAM: Peptidase S16, Lon C-terminal; ATPase, AAA-5; KEGG: mth:MTH785 ATP-dependent protease Lon; SMART: ATPase, AAA+ type, core; Belongs to the peptidase S16 family.
  
  
 0.650
Your Current Organism:
Methanobacterium lacus
NCBI taxonomy Id: 877455
Other names: DSM 24406, JCM 17760, M. lacus, Methanobacterium lacus Borrel et al. 2012, Methanobacterium sp. 17A1, Methanobacterium sp. AL-21, strain 17A1
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