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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hslUHeat 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. (469 aa)    
Predicted Functional Partners:
hslV
ATP dependent peptidase CodWX, CodW component; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
 0.999
codY
GTP-sensing pleiotropic transcriptional repressor CodY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family.
 
  
 0.944
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 [...]
  
  
 0.919
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
  
 0.853
lon
ATP-dependent proteinase; 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.
  
  
 0.839
Toce_2123
ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR018368:IPR001270:IPR004176:IPR 003959:IPR001943:IPR013093:IPR019489; KEGG: tte:TTE2327 ATPase with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associat [...]
  
  
 0.817
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 [...]
   
 
 0.816
xerC
Tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
  
  
 0.793
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
  
 0.774
Toce_0907
COGs: COG0459 Chaperonin GroEL (HSP60 family); InterPro IPR002194:IPR017998:IPR002423; KEGG: pth:PTH_0876 chaperonin GroEL; PFAM: chaperonin Cpn60/TCP-1; SPTR: Chaperonin Cpn60/TCP-1; PFAM: TCP-1/cpn60 chaperonin family.
   
  
 0.774
Your Current Organism:
Thermosediminibacter oceani
NCBI taxonomy Id: 555079
Other names: T. oceani DSM 16646, Thermosediminibacter oceani DSM 16646, Thermosediminibacter oceani JW/IW-1228P, Thermosediminibacter oceani str. DSM 16646, Thermosediminibacter oceani strain DSM 16646
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