close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
AEB85099.1SMART: TRASH; TIGRFAM: ATPase, P-type, heavy metal translocating; ATPase, P type, cation/copper-transporter; ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter; KEGG: lbf:LBF_0420 cation transport ATPase; PFAM: ATPase, P-type, ATPase-associated domain; YHS; Haloacid dehalogenase-like hydrolase. (777 aa)    
Predicted Functional Partners:
AEB85100.1
KEGG: lbf:LBF_0421 hypothetical protein.
 
     0.841
AEB85101.1
KEGG: ajs:Ajs_1467 heavy metal transport/detoxification protein; manually curated; PFAM: Heavy metal transport/detoxification protein.
  
 
 0.799
AEB82699.1
KEGG: azo:azo2443 phenol hydroxylase subunit P1; PFAM: Methane/phenol/toluene hydroxylase.
   
 
 0.788
AEB84205.1
TIGRFAM: ATPase, P-type, heavy metal translocating; ATPase, P-type, heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating; ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter; KEGG: tin:Tint_3215 heavy metal translocating P-type ATPase; PFAM: ATPase, P-type, ATPase-associated domain; Haloacid dehalogenase-like hydrolase.
 
 
0.736
merA-2
Mercuric reductase; Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
  
 
 0.736
AEB85098.1
KEGG: ajs:Ajs_1470 hypothetical protein.
     
 0.733
AEB85084.1
TIGRFAM: ATPase, P type, cation/copper-transporter; ATPase, P-type, heavy metal translocating; ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter; KEGG: ajs:Ajs_2696 copper-translocating P-type ATPase; PFAM: ATPase, P-type, ATPase-associated domain; Haloacid dehalogenase-like hydrolase.
 
 
0.705
AEB85704.1
Heavy metal translocating P-type ATPase; PFAM: ATPase, P-type, ATPase-associated domain; Haloacid dehalogenase-like hydrolase; manually curated; KEGG: ajs:Ajs_1513 heavy metal translocating P-type ATPase; TIGRFAM: ATPase, P-type, heavy metal translocating; ATPase, P type, cation/copper-transporter; ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter.
 
 
0.705
AEB82700.1
PFAM: Monooxygenase component MmoB/DmpM; KEGG: azo:azo2442 phenol hydrolase subunit P2.
   
 
 0.657
AEB82702.1
PFAM: Phenol hydroxylase,conserved region; KEGG: rpf:Rpic12D_3551 phenol hydroxylase conserved region.
   
 
 0.657
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
Server load: low (38%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.