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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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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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lon-3ATP-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. (812 aa)    
Predicted Functional Partners:
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.802
Deba_3228
Heat shock protein Hsp20; COGs: COG0071 Molecular chaperone (small heat shock protein); InterPro IPR008978:IPR002068; KEGG: afr:AFE_2086 heat shock protein, HSP20 family; PFAM: heat shock protein Hsp20; SPTR: B7J4U6 Heat shock protein, Hsp20 family; PFAM: Hsp20/alpha crystallin family; Belongs to the small heat shock protein (HSP20) family.
  
  
 0.787
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 [...]
  
 
 0.784
hslU
Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
  
  
 0.772
grpE
GrpE 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. Several rounds of ATP-dependent i [...]
  
  
 0.751
hslV
20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.738
Deba_3133
Short-chain dehydrogenase/reductase SDR; COGs: COG3425 3-hydroxy-3-methylglutaryl CoA synthase; InterProIPR016040:IPR016039:IPR016083:IPR013747:IPR 002878:IPR002198:IPR003033:IPR002347; KEGG: dol:Dole_1550 short-chain dehydrogenase/reductase SDR; PFAM: short-chain dehydrogenase/reductase SDR; protein of unknown function DUF35; 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III domain protein; Sterol-binding domain protein; SPTR: A8ZZV4 Short-chain dehydrogenase/reductase SDR; PFAM: Rubredoxin-like zinc ribbon domain (DUF35_N); 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C term [...]
  
 0.735
Deba_2571
ATP-binding region ATPase domain protein; InterPro IPR003594; KEGG: sfu:Sfum_3853 hypothetical protein; PFAM: ATP-binding region ATPase domain protein; SPTR: A0LQ20 Putative uncharacterized protein; PFAM: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.
   
 
 0.721
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.
  
 
 0.717
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.703
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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