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
kefFK+/H+ antiporter, ancillary protein KefF, also called Glutathione-regulated potassium-efflux system ancillary protein is required for full activity of KefC. This ancillary protein stimulates transport activity of KefC about 10-fold. It is unlikely that kefF has oxidoreductase activity, it has probably evolved from its function as oxidoreductase to be regulator of kefC; Belongs to the NAD(P)H dehydrogenase (quinone) family; Localized in the cytoplasm; High confidence in function and specificity. (201 aa)    
Predicted Functional Partners:
kefC
The K(+)/H(+) antiporter KefC is a Glutathione-regulated potassium-efflux system protein responsible for glutathione-gated K+ efflux. Activation of KefC K+ efflux system only occurs in the presence of glutathione and a reactive electrophile such as methylglyoxal or N-ethylmaleimide. KefC is important for cell survival during exposure to toxic metabolites, possibly because they can release K+, allowing H+ uptake. H+ uptake (acidification of the cytoplasm) accompanying or following K+ efflux may serve as a further protective mechanism against electrophile toxicity; Contains 12 transmembr [...]
 
 0.995
CAZ98392.1
Conserved hypothetical protein; Protein that consists of an TfoX module found in the N-terminal part of the tfoX gene product required for DNA transformation; Localized in the cytoplasm.
       0.757
wrbA
NAD(P)H dehydrogenase [quinone]; The enzyme catalyse the NAD(P)H-dependent two-electron reductions of quinones; It apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons to protect cells against damage by free radicals and reactive oxygen species; It has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone; Uses a FAD cofactor; Localized in the cytoplasm; High confidence in function and specificity.
  
     0.660
lysA
Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine.
    
  0.593
CAZ98389.1
Putative protein.
       0.553
CAZ95729.1
Sodium/hydrogen exchanger; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. This integral membrane protein also contains a C-terminal TrkA- N domain which binds NAD and adopts a Rossmann fold; Contains twelve transmembrane helices; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter family; Localized in the cytoplasmic membrane; Specificity unclear.
 
 
 0.549
CAZ95864.1
Aminotransferases use the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Specificity unclear.
   
    0.465
aatB
Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.
   
    0.465
aatA-2
Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.
   
    0.465
CAZ94893.1
Aminotransferases use the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Specificity unclear.
   
    0.465
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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