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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AEJ60430.1Peptidoglycan-binding lysin domain-containing protein; PFAM: LysM domain; InterPro IPR018392:IPR002482; KEGG: sta:STHERM_c01550 hypothetical protein; PFAM: Peptidoglycan-binding lysin domain; SMART: Peptidoglycan-binding Lysin subgroup; SPTR: Peptidoglycan-binding lysin domain. (334 aa)    
Predicted Functional Partners:
htpG
Chaperone protein htpG; Molecular chaperone. Has ATPase activity.
  
 0.933
grpE
Protein grpE; 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 [...]
  
 
 0.921
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.900
AEJ60847.1
Heat shock protein DnaJ domain protein; PFAM: DnaJ domain; InterPro IPR001623; KEGG: sta:STHERM_c05450 hypothetical protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal; SPTR: Heat shock protein DnaJ domain protein.
  
 0.870
AEJ61281.1
Heat shock protein DnaJ domain protein; PFAM: DnaJ domain; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: sta:STHERM_c09840 molecular chaperone protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal; SPTR: Heat shock protein DnaJ domain protein.
  
 0.870
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 [...]
  
 0.870
AEJ61170.1
ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associated with various cellular activities (AAA); TIGRFAM: ATP-dependent Clp protease ATP-binding subunit clpA; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR013461:IPR004176:IPR003959:IPR013093:IPR 019489:IPR003593; KEGG: sta:STHERM_c12610 ClpA-like protein; PFAM: ATPase associated with various cellular activities, AAA-2; ATPase, AAA-type, core; Clp, N-terminal; Clp ATPase, C-ter [...]
  
 
 0.844
AEJ61541.1
ATPase AAA-2 domain protein; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR004176:IPR003959:IPR001943:IPR 013093:IPR019489; KEGG: sta:STHERM_c12380 chaperone ClpB; PFAM: ATPase associated with various cellular activities, AAA-2; ATPase, AAA-type, core; Clp, N-terminal; UvrB/UvrC protein; Clp ATPase, C-terminal; SMART: ATPase, AAA+ type, core; SPTR: ATPase AA [...]
  
 
 0.844
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.
  
 
 0.844
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.825
Your Current Organism:
Spirochaeta thermophila
NCBI taxonomy Id: 869211
Other names: S. thermophila DSM 6578, Spirochaeta thermophila DSM 6578, Spirochaeta thermophila str. DSM 6578, Spirochaeta thermophila strain DSM 6578
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