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
Nham_1007Multisubunit potassium/proton antiporter, PhaE subunit; TC 2.A.63.1.1. (162 aa)    
Predicted Functional Partners:
Nham_1005
Multisubunit potassium/proton antiporter, PhaG subunit; TC 2.A.63.1.1.
 
 
 0.999
Nham_1006
Multisubunit potassium/proton antiporter, PhaF subunit; TC 2.A.63.1.1.
 
 
 0.999
Nham_1008
Multisubunit potassium/proton antiporter, PhaD subunit; TC 2.A.63.1.1.
 
 0.999
Nham_1009
Multisubunit potassium/proton antiporter, PhaC subunit; TC 2.A.63.1.1.
 
 
 0.999
Nham_1010
Multicomponent K+:H+ antiporter subunit A; TC 2.A.63.1.1; TC 2.A.63.1.1.
 
 
 0.999
Nham_2209
NADH dehydrogenase subunit L.
  
 
 0.904
nuoI
NADH dehydrogenase subunit I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
   
 
 0.499
mutM-2
DNA-(apurinic or apyrimidinic site) lyase / Formamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
  
    0.478
nuoC
NADH dehydrogenase subunit C; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family.
   
   0.448
nuoB
NADH dehydrogenase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
   
   0.448
Your Current Organism:
Nitrobacter hamburgensis
NCBI taxonomy Id: 323097
Other names: N. hamburgensis X14, Nitrobacter hamburgensis X14, Nitrobacter hamburgensis str. X14, Nitrobacter hamburgensis strain X14
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