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
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[Homology]
Score
hslO33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. (298 aa)    
Predicted Functional Partners:
APR08025.1
Heat shock protein 15.
  
  
 0.783
ftsH
ATP-dependent zinc metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
  
  
 0.782
APR08032.1
tRNA-dihydrouridine synthase C; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family.
  
  
 0.736
hslV
ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.686
lysS
Lysine--tRNA ligase; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
  
 0.653
APR08481.1
ATP-dependent protease ATPase subunit ClpY; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity.
   
  
 0.578
APR08029.1
Hypoxanthine-guanine phosphoribosyltransferase; Belongs to the purine/pyrimidine phosphoribosyltransferase family.
       0.576
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 [...]
  
  
 0.576
tilS
tRNA(Ile)-lysidine synthase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
       0.573
grpE
Heat shock 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- [...]
   
  
 0.542
Your Current Organism:
Lactobacillus parabuchneri
NCBI taxonomy Id: 152331
Other names: ATCC 49374, CCUG 32261, CIP 103368, CIP 106749 [[Lactobacillus ferintoshensis Simpson et al. 2002]], DSM 5707, JCM 12493, JCM 12511 [[Lactobacillus ferintoshensis Simpson et al. 2002]], L. parabuchneri, LMG 11457, LMG:11457, Lactobacillus ferintoshensis, Lactobacillus ferintoshensis Simpson et al. 2002, NBRC 107865, NCDO 2748, NCIMB 8838, strain R7-84 [[Lactobacillus ferintoshensis Simpson et al. 2002]], strain R7-84(T) [[Lactobacillus ferintoshensis Simpson et al. 2002]]
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