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.
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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
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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
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[Homology]
Score
BBAL3_3209Hypothetical protein; [O] COG0330 Membrane protease subunits, stomatin/prohibitin homologs. (323 aa)    
Predicted Functional Partners:
ftsH
ATP-dependent metallopeptidase HflB subfamily; 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. In the central section; belongs to the AAA ATPase family.
  
 0.910
BBAL3_719
[R] COG0790 FOG: TPR repeat, SEL1 subfamily.
  
 
  0.809
nuoC
NADH (or F420H2) dehydrogenase, subunit C subfamily, putative; 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.
   
  0.711
BBAL3_1728
Efflux ABC transporter, permease protein; [V] COG0577 ABC-type antimicrobial peptide transport system, permease component.
  
     0.691
nuoD
NADH dehydrogenase (quinone), D subunit; 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 49 kDa subunit family.
   
  0.683
BBAL3_2206
Uncharacterized domain HDIG protein; [R] COG3481 Predicted HD-superfamily hydrolase.
  
     0.673
nuoI
NADH-quinone oxidoreductase, chain I subfamily; 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.
   
  0.667
BBAL3_3083
NADH dehydrogenase (quinone), G subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family.
   
  0.658
BBAL3_2810
Vesicle transport v-SNARE protein; [M] COG0739 Membrane proteins related to metalloendopeptidases.
  
 
   0.649
BBAL3_3218
NADH oxidoreductase (quinone), F subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
 0.647
Your Current Organism:
Brevundimonas sp. BAL3
NCBI taxonomy Id: 391600
Other names: B. sp. BAL3
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