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
msrPMononuclear molybdenum enzyme YedY; 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 bot [...] (331 aa)    
Predicted Functional Partners:
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 [...]
 
  
 0.979
AKM32730.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.871
AKM30977.2
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).
   
 
 0.504
AOX47837.1
Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
 
 0.479
AKM30314.1
C-type cytochrome biogenesis protein CcsB; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.469
AKM30315.2
Cytochrome C biogenesis protein ResB; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.464
AKM32604.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.402
Your Current Organism:
Pandoraea faecigallinarum
NCBI taxonomy Id: 656179
Other names: CCM 2766, DSM 23572, NBRC 106092, P. faecigallinarum, Pandoraea faecigallinarum Sahin et al. 2011, Pandoraea sp. KOx, strain KOx
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