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msrA protein (Escherichia coli K12 DH10B) - STRING interaction network
"msrA" - Methionine sulfoxide reductase A in Escherichia coli K12 DH10B
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query proteins and first shell of interactors
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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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msrAMethionine sulfoxide reductase A; Could have 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 (212 aa)    
Predicted Functional Partners:
msrB
Methionine sulfoxide reductase B (137 aa)
 
  0.994
tamB
Hypothetical protein; Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane (1259 aa)
              0.565
tamA
Outer membrane protein; Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Has anion selective channel-forming ability, but the physiological relevance of this activity is unclear (577 aa)
              0.559
trxA
Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (109 aa)
   
  0.558
trxC
Thioredoxin 2; Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin (139 aa)
   
  0.558
ytfP
Hypothetical protein; May play a role in antibiotic biosynthesis (113 aa)
              0.549
dsbA
Protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway (208 aa)
   
  0.547
dsbE
Periplasmic thioredoxin of cytochrome c-type biogenesis; Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase. DsbE is maintained in a reduced state by DsbD (185 aa)
   
  0.547
metB
Cystathionine gamma-synthase; Catalyzes the formation of L-cystathionine from O- succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma- replacement reaction. In the absence of thiol, catalyzes gamma- elimination to form 2-oxobutanoate, succinate and ammonia (386 aa)
   
 
  0.501
metC
Cystathionine beta-lyase (395 aa)
   
 
  0.501
Your Current Organism:
Escherichia coli K12 DH10B
NCBI taxonomy Id: 316385
Other names: E. coli str. K-12 substr. DH10B, Escherichia coli DH10B, Escherichia coli K12 DH10B, Escherichia coli str. K-12 substr. DH10B, Escherichia coli str. K12 substr. DH10B, Escherichia coli strain K12 substrain DH10B
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