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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
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Coexpression
Experiments
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[Homology]
Score
KYC_08095Glycosyl transferase family protein. (639 aa)    
Predicted Functional Partners:
KYC_06400
COG1501 Alpha-glucosidases, family 31 of glycosyl hydrolases; Belongs to the glycosyl hydrolase 31 family.
    
 
 0.680
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 [...]
    
 
 0.644
KYC_13392
DnaJ domain-containing protein; COG2214 DnaJ-class molecular chaperone.
    
 
 0.644
secY
Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
   
 
 0.556
KYC_08100
Rhamnan synthesis F; COG0438 Glycosyltransferase.
   
   0.527
KYC_08135
COG0463 Glycosyltransferases involved in cell wall biogenesis.
   
 
 0.485
Your Current Organism:
Achromobacter arsenitoxydans
NCBI taxonomy Id: 477184
Other names: A. arsenitoxydans SY8, Achromobacter arsenitoxydans SY8, Achromobacter arsenitoxydans str. SY8, Achromobacter arsenitoxydans strain SY8, Achromobacter sp. SY8, arsenite-oxidizing bacterium SY8
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