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.
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]
Score
cbpADnaJ domain protein; KEGG: apb:SAR116_1614 3.3e-34 DnaJ family molecular chaperone K03686; Psort location: Cytoplasmic, score: 9.67. (306 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.996
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity.
  
 0.945
grpE
Co-chaperone 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-depend [...]
 
 
 0.927
KXA31478.1
Tetratricopeptide repeat protein; KEGG: btl:BALH_3160 6.2e-05 response regulator aspartate phosphatase K06361; Psort location: Cytoplasmic, score: 7.50.
 
 
 0.922
clpB
ATP-dependent chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.
 
 
 0.900
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.839
fusA_2
KEGG: acl:ACL_0298 6.7e-171 fusA; translation elongation factor EF-G K02355; Psort location: Cytoplasmic, score: 9.97.
 
 0.827
KXA30502.1
Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
 
 
 0.810
resA_2
Redoxin family protein; KEGG: aca:ACP_1678 1.6e-11 thiol-disulfide oxidoreductase.
   
 0.787
rplQ
Ribosomal protein L17; KEGG: apb:SAR116_2416 1.5e-22 50S ribosomal protein L17 K02879; Psort location: Cytoplasmic, score: 9.97.
  
 
 0.765
Your Current Organism:
Peptoniphilus harei
NCBI taxonomy Id: 54005
Other names: ATCC BAA-601, CCUG 38491, CIP 105323, DSM 10020, NCTC 13076, P. harei, Peptostreptococcus harei, Schleiferella harei
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