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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
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[Homology]
Score
msrPOxidoreductase molybdopterin binding 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 [...] (331 aa)    
Predicted Functional Partners:
msrQ
Ferric reductase domain protein protein transmembrane component domain 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. MsrQ provides electrons for re [...]
 
  
 0.990
ADN56349.1
KEGG: bpy:Bphyt_0625 gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I.
   
 
 0.822
ADN59970.1
KEGG: bph:Bphy_4792 cytochrome c oxidase, subunit II; TIGRFAM: cytochrome c oxidase, subunit II; PFAM: cytochrome c oxidase subunit II; cytochrome c class I.
  
 
 0.610
ADN59154.1
KEGG: bxe:Bxe_A0348 cytochrome c assembly protein; TIGRFAM: cytochrome c-type biogenesis protein CcsB; PFAM: cytochrome c assembly protein.
       0.510
ADN59155.1
KEGG: bxe:Bxe_A0347 cytochrome c biogenesis protein.
       0.510
ADN57338.1
KEGG: bpy:Bphyt_6318 putative cytochrome c552.
 
 
 
 0.454
ADN57886.1
TIGRFAM: hydroxyisourate hydrolase; KEGG: bpy:Bphyt_2324 hydroxyisourate hydrolase; PFAM: Transthyretin; Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily.
   
   0.441
ADN57495.1
PFAM: molybdopterin biosynthesis MoaE protein; KEGG: bxe:Bxe_A2377 molybdopterin synthase subunit MoaE.
 
   
 0.436
ADN56282.1
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).
   
 
 0.416
ADN57273.1
PFAM: outer membrane chaperone Skp (OmpH); KEGG: bxe:Bxe_A1691 outer membrane protein (OmpH-like); Belongs to the skp family.
      
 0.408
Your Current Organism:
Burkholderia sp. CCGE1003
NCBI taxonomy Id: 640512
Other names: B. sp. CCGE1003
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