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:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ADW18184.1COGs: COG0740 Protease subunit of ATP-dependent Clp protease; InterPro IPR001907: IPR018215; KEGG: dps:DP2538 ATP-dependent Clp protease, proteolytic subunit (ClpP); PFAM: peptidase S14 ClpP; PRIAM: Endopeptidase Clp; SPTR: ATP-dependent Clp protease proteolytic subunit; TIGRFAM: ATP-dependent Clp protease, proteolytic subunit ClpP; PFAM: Clp protease; TIGRFAM: ATP-dependent Clp protease, proteolytic subunit ClpP. (200 aa)    
Predicted Functional Partners:
ADW18185.1
COGs: COG1219 ATP-dependent protease Clp ATPase subunit; InterProIPR004487: IPR017948: IPR010603: IPR013093: IPR 019489: IPR003593; KEGG: dak:DaAHT2_1302 ATP-dependent Clp protease, ATP-binding subunit ClpX; PFAM: ATPase AAA-2 domain protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATP-dependent Clp protease, ATP-binding subunit ClpX; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit ClpX; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; ClpX C4-type zinc finger; TIGRFAM: endopeptidase Clp ATP-binding regulatory subunit (clpX).
 0.999
clpB
ATP-dependent chaperone 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; Belongs to the ClpA/ClpB family.
 
 
 0.896
clpA
ATP-dependent Clp protease ATP-binding subunit ClpA; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR004176: IPR003959: IPR013093: IPR019489: IPR 001270: IPR018368: IPR003593: IPR013461; KEGG: dak:DaAHT2_2492 ATP-dependent Clp protease, ATP-binding subunit ClpA; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; Clp domain protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATP-dependent Clp protease, ATP-binding subunit clpA; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA domain (Cdc48 subfamily); Clp amino termi [...]
 
 
 0.891
ADW18186.1
COGs: COG0466 ATP-dependent Lon protease; InterProIPR001984: IPR008268: IPR004815: IPR003111: IPR 003959: IPR003593; KEGG: dak:DaAHT2_1301 ATP-dependent protease La; PFAM: peptidase S16 lon domain protein; AAA ATPase central domain protein; PRIAM: Endopeptidase La; SMART: peptidase S16 lon domain protein; AAA ATPase; SPTR: ATP-dependent protease La; TIGRFAM: ATP-dependent protease La; PFAM: ATP-dependent protease La (LON) domain; ATPase family associated with various cellular activities (AAA); Lon protease (S16) C-terminal proteolytic domain; TIGRFAM: ATP-dependent protease La.
  
 
 0.888
ADW17752.1
NAD(P)-dependent iron-only hydrogenase diaphorase component flavoprotein; COGs: COG1894 NADH:ubiquinone oxidoreductase NADH-binding (51 kD) subunit; InterProIPR011538: IPR019554: IPR019575: IPR017896: IPR 017900; KEGG: dma:DMR_07840 putative NAD-reducing hydrogenase subunit; PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; PRIAM: NADH dehydrogenase (quinone); SPTR: Putative NAD-reducing hydrogenase subunit; PFAM: NADH-ubiquinone oxidoreductase-F iron-sulfur binding region; 4 [...]
  
 
 0.801
ADW18183.1
Trigger factor; COGs: COG0544 FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor); InterPro IPR005215: IPR008881: IPR001179: IPR008880; KEGG: dak:DaAHT2_1304 trigger factor; PFAM: trigger factor domain-containing protein; peptidylprolyl isomerase FKBP-type; SPTR: Trigger factor; TIGRFAM: trigger factor; PFAM: FKBP-type peptidyl-prolyl cis-trans isomerase; Bacterial trigger factor protein (TF); Bacterial trigger factor protein (TF) C-terminus; TIGRFAM: trigger factor.
 
  
 0.792
ADW16923.1
COGs: COG0749 DNA polymerase I - 3'-5' exonuclease and polymerase domains; InterProIPR020046: IPR020047: IPR002562: IPR001098: IPR 002298: IPR018320: IPR019760: IPR002421: IPR008918; KEGG: dak:DaAHT2_1946 DNA polymerase I; PFAM: DNA-directed DNA polymerase; 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; 3'-5' exonuclease; PRIAM: DNA-directed DNA polymerase; SMART: 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2; 3'-5' exonuclease; DNA-directed DNA polymerase; SPTR: DNA polymerase A; TIGRFAM: DNA polymerase I; PFAM: 5'-3' exonuclea [...]
  
 
 0.791
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.774
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.742
ADW19471.1
COGs: COG0262 Dihydrofolate reductase; InterPro IPR001796: IPR012259: IPR017925; KEGG: gsu:GSU0571 dihydrofolate reductase; PFAM: dihydrofolate reductase region; PRIAM: Dihydrofolate reductase; SPTR: Dihydrofolate reductase; PFAM: Dihydrofolate reductase.
    
 
 0.735
Your Current Organism:
Desulfobulbus propionicus
NCBI taxonomy Id: 577650
Other names: D. propionicus DSM 2032, Desulfobulbus propionicus DSM 2032, Desulfobulbus propionicus str. DSM 2032, Desulfobulbus propionicus strain DSM 2032
Server load: low (10%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.