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.
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from curated databases
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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ClpPProtease subunit of ATP-dependent Clp proteases; 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. (194 aa)    
Predicted Functional Partners:
ClpX
ATP-dependent protease Clp, ATPase subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
 0.998
ClpA-2
ATPase with chaperone activity, ATP-binding subunit; 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.
  
 
 0.933
ClpA
ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family.
  
 
 0.932
Tig
FKBP-type peptidyl-prolyl cis-trans isomerase; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily.
  
 0.914
Lon
ATP-dependent Lon protease; 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.
  
 
 0.843
GroS
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.794
PolA
DNA polymerase I - 3'-5' exonuclease and polymerase domains; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
  
 
 0.759
GroL-2
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.705
ribBA
GTP cyclohydrolase II and 3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family.
   
 
 0.681
PTH_0142
Hypothetical protein; Containing predicted ATPase (COG3899), FhlA, FOG: GAF domain (COG2203), S_TKc, serine/threonine protein kinases, catalytic domain, His Kinase A (phosphoacceptor), HATPase_c, Histidine kinase-like ATPase, REC, signal receiver domain, and ArcB, FOG: HPt domain (COG2198).
  
 0.642
Your Current Organism:
Pelotomaculum thermopropionicum
NCBI taxonomy Id: 370438
Other names: P. thermopropionicum SI, Pelotomaculum thermopropionicum SI, Pelotomaculum thermopropionicum str. SI, Pelotomaculum thermopropionicum strain SI
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