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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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lonATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. (794 aa)    
Predicted Functional Partners:
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. [...]
  
  
 0.826
dnaK
Chaperone protein DnaK; Acts as a chaperone.
  
 0.824
AGB03550.1
Molecular chaperone; PFAM: MreB/Mbl protein; Belongs to the heat shock protein 70 family.
  
 0.824
ileS
isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
   
 
 0.806
AGB03170.1
PFAM: lactate/malate dehydrogenase, alpha/beta C-terminal domain; lactate/malate dehydrogenase, NAD binding domain; Belongs to the LDH/MDH superfamily.
  
 0.797
AGB03685.1
PFAM: lactate/malate dehydrogenase, alpha/beta C-terminal domain; lactate/malate dehydrogenase, NAD binding domain; Belongs to the LDH/MDH superfamily.
  
 0.797
AGB02979.1
Transcriptional regulator; PFAM: MarR family.
     
 0.790
AGB01369.1
PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal.
  
 
 0.784
AGB01782.1
Thermosome subunit; PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal.
  
 
 0.784
AGB03894.1
PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal.
  
 
 0.784
Your Current Organism:
Methanoregula formicica
NCBI taxonomy Id: 593750
Other names: M. formicica SMSP, Methanomicrobiales archaeon SMSP, Methanoregula formicica SMSP, Methanoregula formicica str. SMSP, Methanoregula formicica strain SMSP
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