STRINGSTRING
STRING protein interaction network
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
Slip_1384Heat shock protein Hsp20; COGs: COG0071 Molecular chaperone (small heat shock protein); InterPro IPR008978:IPR002068; KEGG: pth:PTH_1328 molecular chaperone; PFAM: heat shock protein Hsp20; SPTR: A5D2M5 Molecular chaperone; PFAM: Hsp20/alpha crystallin family; Belongs to the small heat shock protein (HSP20) family. (141 aa)    
Predicted Functional Partners:
Slip_2268
ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR001270:IPR003593:IPR001943:IPR004176:IPR 003959:IPR013093:IPR019489:IPR018368; KEGG: swo:Swol_2367 ATPases 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: Q0AUE8 ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; UvrB/uvrC mo [...]
  
 
 0.861
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 [...]
  
  
 0.662
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 [...]
  
 
 0.653
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.645
hslV
20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.503
accD
acetyl-CoA carboxylase, carboxyl transferase, beta subunit; Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA; Belongs to the AccD/PCCB family.
   
  
 0.497
Slip_0302
Molecular chaperone-like protein; COGs: COG0443 Molecular chaperone; KEGG: swo:Swol_0386 molecular chaperone-like protein; SPTR: Q0AZY0 Molecular chaperone-like protein; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family.
  
 
 0.495
Slip_1731
Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023:IPR013126:IPR018181; KEGG: swo:Swol_1452 molecular chaperone DnaK; PFAM: Heat shock protein 70; SPTR: Q0AWZ5 Molecular chaperone DnaK; PFAM: Hsp70 protein.
  
 
 0.495
Slip_2030
KEGG: adg:Adeg_1368 hypothetical protein; SPTR: C9R841 Putative uncharacterized protein.
  
 
 0.495
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.
   
  
 0.493
Your Current Organism:
Syntrophothermus lipocalidus
NCBI taxonomy Id: 643648
Other names: S. lipocalidus DSM 12680, Syntrophothermus lipocalidus DSM 12680, Syntrophothermus lipocalidus TGB-C1, Syntrophothermus lipocalidus str. DSM 12680, Syntrophothermus lipocalidus strain DSM 12680
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