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
ACX96049.1KEGG: rme:Rmet_6344 putative transcriptional regulator MerR; TIGRFAM: Hg(II)-responsive transcriptional regulator; PFAM: Transcription regulator MerR DNA binding; regulatory protein MerR; SMART: regulatory protein MerR. (144 aa)    
Predicted Functional Partners:
ACX96048.1
PFAM: Mercuric transport protein MerT; KEGG: dia:Dtpsy_2130 mercuric transport protein MerT.
 
  
 0.930
merA
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.
 
  
 0.893
merP
Mercuric transport protein periplasmic component; Involved in mercury resistance. Acts as a mercury scavenger that specifically binds to a mercuric ion in the periplasm and probably passes it to the cytoplasmic mercuric reductase MerA via the mercuric transport protein MerT.
 
  
 0.790
ACX94973.1
PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: tgr:Tgr7_2956 heat shock protein DnaJ domain-containing protein.
  
 
 0.758
dnaJ
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, D [...]
  
 
 0.758
rpoB
DNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.719
ACX96884.1
KEGG: tmz:Tmz1t_1845 multi-sensor hybrid histidine kinase; TIGRFAM: PAS sensor protein; PFAM: ATP-binding region ATPase domain protein; response regulator receiver; PAS fold-3 domain protein; GAF domain protein; PAS fold-4 domain protein; PAS fold domain protein; histidine kinase A domain protein; SMART: ATP-binding region ATPase domain protein; histidine kinase A domain protein; response regulator receiver; PAC repeat-containing protein; GAF domain protein; PAS domain containing protein.
   
 
 0.681
rpoA
DNA-directed RNA polymerase, alpha subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.649
rpoZ
DNA-directed RNA polymerase, omega subunit; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
    
   0.647
rpoC
DNA-directed RNA polymerase, beta' subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
   0.647
Your Current Organism:
Halothiobacillus neapolitanus
NCBI taxonomy Id: 555778
Other names: H. neapolitanus c2, Halothiobacillus neapolitanus ATCC 23641, Halothiobacillus neapolitanus c2, Halothiobacillus neapolitanus str. c2, Halothiobacillus neapolitanus strain c2
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