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
KLT20033.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (303 aa)    
Predicted Functional Partners:
KLT19405.1
Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
    
   0.844
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
   
 0.831
dltC
Alanine-phosphoribitol ligase; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
   
 0.831
KLT15308.1
(2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
   0.824
KLT15776.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
   0.821
KLT15482.1
NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
   0.821
KLT15277.1
Fumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
    
  0.786
nuoA
NADH:ubiquinone oxidoreductase subunit A; 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 a menaquinone. 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 subunit 3 family.
    
   0.768
nuoB
NADH dehydrogenase; 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 a menaquinone. 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.
    
   0.758
KLT15479.1
NADH-quinone oxidoreductase subunit C; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
   0.738
Your Current Organism:
Bacillus vireti
NCBI taxonomy Id: 220686
Other names: B. vireti, Bacillus vireti Heyrman et al. 2004, DSM 15602, JCM 21711, LMG 21834, LMG:21834, NBRC 102452, strain IDA3632, strain R-15447
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