STRINGSTRING
htpG htpG dnaJ dnaJ dnaK dnaK hscA hscA BPSS1095 BPSS1095 BPSS1096 BPSS1096 BPSL3080 BPSL3080 fbp-2 fbp-2 BPSL1666 BPSL1666 groL groL ppiA ppiA
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; Molecular chaperone. Has ATPase activity. (632 aa)    
Predicted Functional Partners:
dnaJ
Putative DnaJ chaperone protein; 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 betwee [...]
 
 0.996
dnaK
Putative DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.973
hscA
Chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
  
 0.961
BPSS1095
Similar to Legionella pneumophila chaperone protein DnaK to codon 431 SWALL:DNAK_LEGPN (SWALL:O32482) (644 aa) fasta scores: E(): 1.5e-08, 26.22% id in 328 aa, and to Vibrio cholerae DnaK-related protein vc1374 to codon 611 SWALL:Q9KS85 (EMBL:AE004217) (631 aa) fasta scores: E(): 2.3e-137, 58.09% id in 618 aa, and to Vibrio cholerae DnaK-related protein vc1373 to codon 611 SWALL:Q9KS86 (EMBL:AE004217) (948 aa) fasta scores: E(): 2.9e-67, 39.74% id in 629 aa; Belongs to the heat shock protein 70 family.
  
 0.961
BPSS1096
Similar to Legionella pneumophila chaperone protein DnaK to codon 347 SWALL:DNAK_LEGPN (SWALL:O32482) (644 aa) fasta scores: E(): 3e-06, 25.72% id in 346 aa, and to the full-length Vibrio cholerae DnaK-related protein vc1373 SWALL:Q9KS86 (EMBL:AE004217) (948 aa) fasta scores: E(): 1.3e-84, 47.05% id in 952 aa, and to Vibrio cholerae DnaK-related protein vc1374 to codon 606 SWALL:Q9KS85 (EMBL:AE004217) (631 aa) fasta scores: E(): 1.6e-46, 40.6% id in 628 aa.
  
 0.961
BPSL3080
Putative chaperone protein; Similar to Rhizobium loti DnaK-type molecular chaperone, DnaK Mll5617 SWALL:Q98BE0 (EMBL:AP003007) (418 aa) fasta scores: E(): 1e-61, 44.89% id in 421 aa, and to Chlamydia muridarum chaperone protein DnaK or Tc0675 SWALL:DNAK_CHLMU (SWALL:P56836) (654 aa) fasta scores: E(): 1.7e-05, 26.8% id in 250 aa, and to Vibrio cholerae chaperone protein DnaK or Vc0855 SWALL:DNAK_VIBCH (SWALL:O34241) (635 aa) fasta scores: E(): 2e-05, 26.12% id in 421 aa.
  
 0.960
fbp-2
Similar to Neisseria meningitidis peptidyl-prolyl cis-trans isomerase Fbp or nmb0027 SWALL:FKBP_NEIMB (SWALL:P25138) (109 aa) fasta scores: E(): 2.6e-24, 66.66% id in 105 aa, and to Neurospora crassa FK506-binding protein 9g6.180 SWALL:FKBP_NEUCR (SWALL:P20080) (120 aa) fasta scores: E(): 1.3e-19, 53.5% id in 114 aa.
   
 0.944
BPSL1666
Hypothetical protein; Very low similarities to any database matches to the full length of the CDS. The matches are reduced to the TPR domains that this CDS contains, e.g. Methanosarcina acetivorans TPR-domain containing protein ma1613 SWALL:Q8TQD1 (EMBL:AE010832) (1885 aa) fasta scores: E(): 1.6e-07, 21.22% id in 1164 aa.
  
 0.932
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.930
ppiA
Peptidyl-prolyl cis-trans isomerase A precursor; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
 
 0.928
Your Current Organism:
Burkholderia pseudomallei
NCBI taxonomy Id: 272560
Other names: B. pseudomallei K96243, Burkholderia pseudomallei K96243, Burkholderia pseudomallei str. K96243, Burkholderia pseudomallei strain K96243
Server load: low (28%) [HD]