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
htpGChaperone protein htpG; Molecular chaperone. Has ATPase activity. (629 aa)    
Predicted Functional Partners:
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.994
ppiB
Peptidyl-prolyl cis-trans isomerase, or PPIase or rotamase, accelerates the folding of proteins. It catalyzes the peptidyl-prolyl isomerisation during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilised in the cis conformation in oligopeptides; Contains a N-terminal Cyclophilin type PPIase/CLD and a C-terminal FKBP-type peptidyl-prolyl cis- trans isomerase; Localized in the cytoplasm; High confidence in function and specificity.
  
 0.982
ppiA
Peptidyl-prolyl cis-trans isomerase, or PPIase or rotamase, accelerates the folding of proteins. It catalyzes the peptidyl-prolyl isomerisation during which the peptide bond preceding proline is stabilised in the cis conformation in oligopeptides; Contains a N-terminal Cyclophilin type PPIase/CLD domain and a C-terminal FKBP-type peptidyl-prolyl cis-trans isomerase domain; Signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; High confidence in function and specificity.
  
 0.982
CAZ97540.1
Conserved hypothetical protein; Localized in the cytoplasm.
    
 0.955
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.880
djlA
The protein DjlA is a Regulatory dnaK co-chaperone. Contains a N-terminal transmembrane helix and a C-terminal DnaJ domain; Localized in the cytoplasmic membrane; High confidence in function and specificity.
  
 0.855
CAZ96794.1
Conserved hypothetical membrane protein; Contains three central transmembrane segments; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
  
 0.847
dnaJ
Co-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 [...]
  
 0.847
CAZ97207.1
Hypothetical protein; Contains a N-terminal J domain present in the DnaJ protein; Localized in the cytoplasm.
  
 0.847
cbpA
CbpA is a DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of dnaJ; displays overlapping activities with dnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by dnaK; Contains an N-terminal J domain; Localized in the cytoplasm; High confidence in function and specificity.
  
 0.847
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
Server load: low (36%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.