close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
Swoo_3607Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. (155 aa)    
Predicted Functional Partners:
Swoo_3608
Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.
 
 
 
0.987
hemH
Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.
     
 0.915
Swoo_4187
PFAM: BFD domain protein [2Fe-2S]-binding domain protein; KEGG: spl:Spea_3555 BFD domain protein (2Fe-2S)-binding domain protein.
 
 
 0.860
Swoo_1700
Anti-sigma-factor antagonist; TIGRFAM: anti-anti-sigma factor; PFAM: Sulfate transporter/antisigma-factor antagonist STAS; KEGG: sse:Ssed_2945 anti-sigma-factor antagonist.
   
  
 0.634
Swoo_1961
KEGG: pin:Ping_3719 sensor histidine kinase with ATPase domain; TIGRFAM: PAS sensor protein; PFAM: response regulator receiver; GAF domain protein; ATP-binding region ATPase domain protein; histidine kinase A domain protein; CHASE3 domain protein; PAS fold-4 domain protein; PAS fold domain protein; SMART: PAS domain containing protein.
   
  
 0.555
Swoo_3606
Hypothetical protein.
       0.473
Swoo_2794
PFAM: chemotaxis sensory transducer; CHASE3 domain protein; KEGG: dps:DP0292 chemotaxis transducer.
   
    0.453
nuoC
NADH dehydrogenase I, D subunit; 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
   
    0.436
Your Current Organism:
Shewanella woodyi
NCBI taxonomy Id: 392500
Other names: S. woodyi ATCC 51908, Shewanella woodyi ATCC 51908, Shewanella woodyi str. ATCC 51908, Shewanella woodyi strain ATCC 51908
Server load: medium (44%) [HD]