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
hslOChaperonin HslO; 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. (294 aa)    
Predicted Functional Partners:
KXB56323.1
Methyltransferase domain protein; KEGG: bce:BC4326 1.7e-39 methyltransferase K00599; Psort location: Cytoplasmic, score: 9.97.
 
     0.836
KXB55369.1
S4 domain protein; KEGG: osp:Odosp_1635 1.9e-05 pseudouridine synthase; K06180 23S rRNA pseudouridine1911/1915/1917 synthase.
  
  
 0.773
grpE
Co-chaperone 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-depend [...]
   
  
 0.682
KXB56322.1
Hypothetical protein; KEGG: dat:HRM2_21720 0.00035 map; hypothetical protein K01265; Psort location: Cytoplasmic, score: 8.96.
     
 0.663
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
  
 0.661
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 [...]
  
  
 0.612
KXB54903.1
Putative ribosomal RNA small subunit methyltransferase B; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
 
    0.548
KXB55515.1
Hsp90 protein; KEGG: dme:Dmel_CG1242 1.0e-62 Hsp83; Heat shock protein 83 K04079; Psort location: Cytoplasmic, score: 9.97.
   
  
 0.497
KXB57344.1
Putative fibronectin-binding protein; KEGG: stk:STP_0474 0.00012 v-type sodium ATP synthase subunit I; K02123 V-type H+-transporting ATPase subunit I; Psort location: Cytoplasmic, score: 8.96.
  
     0.492
mrnC
RNase3 domain protein; Involved in correct processing of both the 5' and 3' ends of 23S rRNA precursor. Processes 30S rRNA precursor transcript even in absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller rRNA precursors; Belongs to the MrnC RNase family.
  
     0.490
Your Current Organism:
Lachnoanaerobaculum saburreum
NCBI taxonomy Id: 467210
Other names: ATCC 33271, CCUG 28089, CIP 105341, Catenabacterium saburreum, DSM 3986, Eubacterium saburreum, JCM 11021, L. saburreum, Leptotrichia aerogenes, VPI 11763
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