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
Srot_1900PFAM: peptidase M48 Ste24p; KEGG: mab:MAB_1573c hypothetical protein. (389 aa)    
Predicted Functional Partners:
Srot_1899
TIGRFAM: ribose 5-phosphate isomerase; sugar- phosphate isomerase, RpiB/LacA/LacB family; KEGG: nfa:nfa13270 ribose-5-phosphate isomerase B; PFAM: Ribose/galactose isomerase.
  
    0.650
Srot_2552
PFAM: FAD dependent oxidoreductase; KEGG: mab:MAB_1866c putative oxygenase.
  
     0.482
Srot_1488
PFAM: Protein of unknown function DUF2505; KEGG: gbr:Gbro_0780 protein of unknown function DUF2505.
  
     0.423
grpE
GrpE protein; 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 [...]
  
  
 0.418
Your Current Organism:
Segniliparus rotundus
NCBI taxonomy Id: 640132
Other names: S. rotundus DSM 44985, Segniliparus rotundus ATCC BAA-972, Segniliparus rotundus CIP 108378, Segniliparus rotundus DSM 44985, Segniliparus rotundus JCM 13578, Segniliparus rotundus str. DSM 44985, Segniliparus rotundus strain DSM 44985
Server load: low (12%) [HD]