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
msrPHypothetical protein; 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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S- [...] (332 aa)    
Predicted Functional Partners:
msrQ
Membrane protein, putative; 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 catalytic subunit MsrP, usi [...]
 
  
 0.995
EAQ64493.1
Cytochrome c oxidase, subunit II; 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).
   
 0.875
EAQ66369.1
COG0633 Ferredoxin.
  
 
 0.855
EAQ65664.1
Oxidoreductase, iron-sulfur-binding; COG0543 2-polyprenylphenol hydroxylase and related flavodoxin oxidoreductases.
  
 
 0.855
EAQ65880.1
Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
   
 0.795
EAQ63329.1
Hypothetical protein; COG2010 Cytochrome c, mono- and diheme variants.
   
 0.795
EAQ66696.1
Hypothetical protein.
   
 0.795
EAQ65792.1
Putative Oxidoreductase, FAD-binding; COG0369 Sulfite reductase, alpha subunit (flavoprotein).
     
 0.781
EAQ64138.1
phenylacetate-CoA oxygenase, PaaK subunit; COG1018 Flavodoxin reductases (ferredoxin-NADPH reductases) family 1.
  
 
 0.749
EAQ63849.1
COG1018 Flavodoxin reductases (ferredoxin-NADPH reductases) family 1.
  
 
 0.749
Your Current Organism:
Marinomonas sp. MED121
NCBI taxonomy Id: 314277
Other names: M. sp. MED121
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.