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
msrPTwin-arginine translocation pathway signal; 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 re [...] (340 aa)    
Predicted Functional Partners:
msrQ
Ferric reductase domain protein transmembrane component, N-terminal domain; 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 reduct [...]
 
  
 0.997
Ssed_0198
Cytochrome-c oxidase; 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).
   
 
 0.787
Ssed_4438
KEGG: pat:Patl_3910 hypothetical protein.
   
 
 0.754
Ssed_1106
KEGG: sil:SPOA0154 hypothetical protein.
   
 
 0.708
Ssed_2214
Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
   
 
 0.708
Ssed_0638
KEGG: slo:Shew_0465 hypothetical protein.
   
 
 0.641
Ssed_4058
KEGG: slo:Shew_0516 cytochrome c family protein.
   
 
 0.641
Ssed_0120
Molybdopterin-guanine dinucleotide biosynthesis protein B; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family.
 
 
 
 0.539
Ssed_4398
KEGG: slo:Shew_0091 molybdopterin biosynthesis MoaE.
 
   
 0.538
msrA-2
Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
  
  
 0.503
Your Current Organism:
Shewanella sediminis
NCBI taxonomy Id: 425104
Other names: S. sediminis HAW-EB3, Shewanella sediminis HAW-EB3, Shewanella sediminis str. HAW-EB3, Shewanella sediminis strain HAW-EB3
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.