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
SMF62572.1DMSO/TMAO reductase YedYZ, molybdopterin-dependent catalytic subunit. (257 aa)    
Predicted Functional Partners:
SMF62565.1
Thiosulfate reductase cytochrome b subunit.
 
 
  0.978
SMF55252.1
Cytochrome c oxidase subunit 2.
  
 0.955
msrQ
Sulfoxide reductase heme-binding subunit YedZ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalyti [...]
 
  
 0.923
SMF40723.1
Hypothetical protein.
   
 0.837
SMF78651.1
Hypothetical protein.
   
 0.837
SMF79747.1
Cytochrome c551/c552.
 
 
 0.832
SMF38038.1
Cytochrome c oxidase subunit 2; 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).
   
 0.817
SMF52558.1
Cytochrome c.
   
 0.810
SMF70712.1
Hypothetical protein.
   
 0.810
SMF83077.1
Cytochrome c, mono-and diheme variants.
  
 0.761
Your Current Organism:
Trinickia caryophylli
NCBI taxonomy Id: 28094
Other names: ATCC 25418, Burkholderia caryophylli, CCUG 20834, CFBP 2429, CFBP 3818, CIP 105770, DSM 50341, HAMBI 2159, ICMP 512, JCM 10488, JCM 9310, LMG 2155, LMG:2155, NCPPB 2151, Paraburkholderia caryophylli, Phytomonas caryophylli, Pseudomonas caryophylli, Pseudomonas caryophyllii, T. caryophylli
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.