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
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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
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gene neighborhood
gene co-occurrence
gene fusions
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mleNmalate-H+/Na+-lactate antiporter; Couples proton uptake and Na(+) efflux to the substrate- product malate/lactate antiport, in an electroneutral malate- 2H(+)/Na(+)-lactate exchange. Plays a role in supporting growth to high density on malate at reduced protonmotive force; Belongs to the NhaC Na(+)/H(+) (TC 2.A.35) antiporter family. (468 aa)    
Predicted Functional Partners:
mleA
NAD-dependent malic enzyme (conversion of malate into pyruvate); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
  
    0.946
maeN
Na+/malate symporter; Acts as a Na(+)-malate symporter, as it catalyzes malate- dependent uptake of Na(+) and Na(+)-dependent uptake of malate.
  
  
 0.902
ansB
L-aspartase (aspartate ammonia lyase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II fumarase/aspartase family. Aspartase subfamily.
  
    0.771
ansA
Exported L-asparaginase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the asparaginase 1 family.
 
    0.769
cimH
citrate/malate/H+ symporter; Proton motive force-driven secondary transporter that catalyzes the uptake of both citrate and malate. Appears to be an electroneutral proton-solute symporter; the number of protons transported is equal to the valence of the transported anions. Is strictly stereoselective, translocating only the (S)-enantiomer of malate.
  
   
 0.760
kduD
2-keto-3-deoxygluconate oxidoreductase; Catalyzes the reduction of 2,5-diketo-3-deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3-deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH. Belongs to the short-chain dehydrogenases/reductases (SDR) family.
      
 0.635
yrrI
Putative permease; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.
      
 0.634
ytvI
Putative permease; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.
      
 0.587
yfkE
Putative H+/Ca2+ antiporter; Ca(+)/H(+) antiporter that extrudes calcium in exchange for external protons. Does not transport sodium or potassium. Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. Cation/proton exchanger (CAX) subfamily.
      
 0.583
yhaU
Transporter involved in K+ efflux; Potassium/proton antiporter that mediates the efflux of potassium ions from the cell. Can also mediate rubidium/proton antiport, but has no permeability for sodium or lithium ions. In the absence of KhtT, does not have antiport activity, but can catalyze potassium efflux. Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis, via activation by S-lactoyl-BSH of the antiporter activity, leading to cytoplasmic acidification and methylglyoxal resistance ; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transpo [...]
      
 0.530
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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