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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[Homology]
Score
hslUMolecular chaperone and ATPase component of HslUV protease; 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. (442 aa)    
Predicted Functional Partners:
hslV
Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
 
 0.999
grpE
Protein GrpE, Heat Shock Chaperone (HSP-70 cofactor); 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 [...]
  
  
 0.931
groL
Cpn60 chaperonin GroEL, large subunit of GroESL(Chaperonin Cpn60/TCP-1,23-525); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
  
 0.916
htpG
Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity.
   
  
 0.907
groES
Cpn10 chaperonin GroES, small subunit of GroESL(Chaperonin Cpn10,1-95); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
  
 0.907
lon
DNA-binding ATP-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.
  
  
 0.891
XM1_0855
Putative Thioredoxin domain-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
 
 0.890
XM1_0183
Conserved protein of unknown function（DnaJ N-terminal domain-containing protein） Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure.
   
 
 0.764
dnaJ
Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...]
   
 
 0.764
XM1_4448
DnaJ-class molecular chaperone; Function of strongly homologous gene; factor.
   
 
 0.764
Your Current Organism:
Magnetospirillum sp. XM1
NCBI taxonomy Id: 1663591
Other names: M. sp. XM-1, Magnetospirillum sp. XM-1
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