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
Olsu_1663COGs: COG0783 DNA-binding ferritin-like protein (oxidative damage protectant); InterPro IPR008331:IPR009078:IPR012347:IPR002177; KEGG: fnu:FN1079 neutrophil-activating protein A; PFAM: Ferritin Dps family protein; SPTR: A8RN70 Putative uncharacterized protein; PFAM: Ferritin-like domain; Belongs to the Dps family. (147 aa)    
Predicted Functional Partners:
Olsu_1662
Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family.
  
  
 0.688
Olsu_0499
COGs: COG0674 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductase alpha subunit; InterProIPR011895:IPR017900:IPR002880:IPR019752:IPR 019456:IPR001450:IPR002869:IPR009014:IPR015941:IPR017896; KEGG: apv:Apar_1328 pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin iron-sulfur binding domain protein; SPTR: B6GD95 Putative uncharacterized protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxido [...]
    
 
 0.680
Olsu_1341
Heavy metal translocating P-type ATPase; COGs: COG2217 Cation transport ATPase; InterProIPR006121:IPR001757:IPR000695:IPR006403:IPR 006416:IPR001969:IPR018303:IPR017969:IPR008250:IPR005834; KEGG: apv:Apar_0439 heavy metal translocating P-type ATPase; PFAM: E1-E2 ATPase-associated domain protein; Heavy metal transport/detoxification protein; Haloacid dehalogenase domain protein hydrolase; SPTR: C8W9T2 Heavy metal translocating P-type ATPase; TIGRFAM: heavy metal translocating P-type ATPase; copper-translocating P-type ATPase; ATPase, P-type (transporting), HAD superfamily, subfamily IC; [...]
  
  
 0.588
Olsu_0658
Peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
  
  
 0.570
Olsu_0520
COGs: COG0655 Multimeric flavodoxin WrbA; KEGG: bhy:BHWA1_02501 multimeric flavodoxin WrbA fused to cytochrome c-like domain; SPTR: C1QEI5 Multimeric flavodoxin WrbA; PFAM: NADPH-dependent FMN reductase.
  
  
 0.497
Olsu_1009
Conserved hypothetical protein; COGs: COG0655 Multimeric flavodoxin WrbA; KEGG: cdf:CD3637 hypothetical protein; SPTR: C6PUJ0 NADPH-dependent FMN reductase; PFAM: NADPH-dependent FMN reductase.
  
  
 0.497
hpf
SSU ribosomal protein S30P;sigma 54 modulation protein; Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth.
  
  
 0.481
Your Current Organism:
Olsenella uli
NCBI taxonomy Id: 633147
Other names: O. uli DSM 7084, Olsenella uli ATCC 49627, Olsenella uli DSM 7084, Olsenella uli str. DSM 7084, Olsenella uli strain DSM 7084
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.