STRINGSTRING
htpX protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"htpX" - Protease HtpX homolog in Desulfovibrio vulgaris Hildenborough
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
htpXProtease HtpX homolog; Identified by match to protein family HMM PF01435; Belongs to the peptidase M48B family (286 aa)    
Predicted Functional Partners:
DVU_2495
Identified by match to protein family HMM PF03061; match to protein family HMM TIGR00369 (177 aa)
         
  0.650
polA
DNA polymerase I; Identified by similarity to SP-P00582; match to protein family HMM PF00476; match to protein family HMM PF01367; match to protein family HMM PF02739; match to protein family HMM TIGR00593 (1015 aa)
         
  0.647
DVU_0414
NADP-dependent malic enzyme-related protein; Identified by match to protein family HMM PF00390; match to protein family HMM PF03949 (439 aa)
       
  0.583
dnaK
Chaperone protein DnaK; Acts as a chaperone (636 aa)
   
 
  0.582
clpB
Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity); Belongs to the ClpA/ClpB family (865 aa)
   
   
  0.568
ftsH
ATP-dependent zinc metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family (656 aa)
   
 
  0.562
DVU_2470
Membrane protein, putaive; Identified by similarity to SP-P75768; match to protein family HMM PF01027; Belongs to the BI1 family (233 aa)
   
   
  0.552
DVU_2496
annotation not available (150 aa)
              0.550
groEL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (547 aa)
   
   
  0.535
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity; Belongs to the heat shock protein 90 family (637 aa)
   
   
  0.529
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
Server load: low (17%) [HD]