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
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.
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from curated databases
textmining
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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clpPEndopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (219 aa)    
Predicted Functional Partners:
clpX
Sigma 54 interacting domain protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
 0.999
Coch_2099
PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Torsin; ATPase associated with various cellular activities AAA_5; Clp domain protein; SMART: AAA ATPase; KEGG: fps:FP0747 ATPase with chaperone activity ATP- binding subunit; Belongs to the ClpA/ClpB family.
 
 
 0.862
clpB
ATP-dependent chaperone 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.
 
 
 0.858
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.808
lon
ATP-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.
  
 
 0.708
Coch_0969
KEGG: fjo:Fjoh_0367 citrate synthase I; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; Belongs to the citrate synthase family.
   
 0.678
Coch_0136
PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: gfo:GFO_1472 ferredoxin-like protein.
   
 
 0.674
def
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
 
  
 0.671
atpA
ATP synthase F1, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.
   
 0.671
Coch_2011
KEGG: gfo:GFO_1404 thioredoxin-like protein.
  
 
 0.664
Your Current Organism:
Capnocytophaga ochracea
NCBI taxonomy Id: 521097
Other names: C. ochracea DSM 7271, Capnocytophaga ochracea ATCC 27872, Capnocytophaga ochracea DSM 7271, Capnocytophaga ochracea str. DSM 7271, Capnocytophaga ochracea strain DSM 7271
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