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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Ljam_2506Bleomycin resistance protein. (124 aa)    
Predicted Functional Partners:
Ljam_2507
Transcriptional regulator.
     0.976
Ljam_0503
Polyketide synthase.
  
 0.744
Ljam_1060
Polyketide synthase.
  
 0.744
Ljam_2505
Transcription activator.
       0.736
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.
   
 
  0.636
korA
2-oxoglutarate ferredoxin oxidoreductase subunit alpha.
     
 0.566
Ljam_1622
Succinate dehydrogenase cytochrome b556 subunit C.
   
    0.500
nuoD
NADH dehydrogenase I subunit D; 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.
   
    0.500
Ljam_2622
Oxaloacetate decarboxylase subunit alpha.
    
  0.477
birA
biotin-[acetylCoA carboxylase] holoenzyme synthetase and biotin operon repressor; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
  
    0.463
Your Current Organism:
Legionella jamestowniensis
NCBI taxonomy Id: 455
Other names: ATCC 35298, CCUG 29669, CIP 103845, DSM 19215, JCM 7590, L. jamestowniensis, Legionella jamestownensis, NCTC 11981, strain JA-26-G1-E2
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