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msrP protein (Methylobacter tundripaludum) - STRING interaction network
"msrP" - Protein-methionine-sulfoxide reductase catalytic subunit MsrP in Methylobacter tundripaludum
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
msrPProtein-methionine-sulfoxide reductase catalytic subunit MsrP; 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-stereospecifi [...] (314 aa)    
Predicted Functional Partners:
msrQ
Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; 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 [...] (203 aa)
 
   
  0.994
Mettu_0982
Uncharacterized protein; KEGG- hba-Hbal_0248 glucose sorbosone dehydrogenase (668 aa)
     
  0.942
Mettu_0222
KEGG- mes-Meso_2793 cytochrome c, class I (380 aa)
     
  0.924
Mettu_2031
KEGG- cytochrome c family protein (134 aa)
     
  0.906
Mettu_0259
PFAM- Cytochrome c oxidase subunit II C-terminal; KEGG- nmu-Nmul_A0460 cytochrome c oxidase, subunit II (348 aa)
     
  0.829
Mettu_0221
KEGG- smd-Smed_4760 cytochrome c oxidase subunit II; TIGRFAM- Cytochrome c oxidase, subunit II; PFAM- Cytochrome c oxidase subunit II C-terminal; Cytochrome c, class I (326 aa)
     
  0.829
Mettu_0140
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) (384 aa)
     
  0.829
Mettu_1427
Sensor protein; Member of a two-component regulatory system (463 aa)
       
  0.732
Mettu_3569
3-mercaptopyruvate sulfurtransferase; PFAM- Rhodanese-like; KEGG- rmr-Rmar_0188 rhodanese domain protein; SMART- Rhodanese-like (281 aa)
   
 
  0.725
Mettu_3239
PFAM- Cytochrome d1, haem region; Cytochrome c, class I; KEGG- rme-Rmet_3331 cytochrome d1, heme region (526 aa)
     
  0.718
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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