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JG24_20020 protein (Klebsiella pneumoniae) - STRING interaction network
"JG24_20020" - DNA mismatch repair protein MutS in Klebsiella pneumoniae
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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
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some 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
JG24_20020DNA mismatch repair protein MutS; This protein performs the mismatch recognition step during the DNA repair process; Derived by automated computational analysis using gene prediction method- Protein Homology (853 aa)    
Predicted Functional Partners:
JG24_27905
DNA mismatch repair protein MutL; Derived by automated computational analysis using gene prediction method- Protein Homology (619 aa)
 
 
  0.990
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
 
 
  0.872
JG24_08295
Transcription-repair coupling factor; Derived by automated computational analysis using gene prediction method- Protein Homology (1148 aa)
   
   
  0.784
ruvA
Holliday junction ATP-dependent DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB (203 aa)
 
     
  0.779
JG24_25485
DNA polymerase III beta subunit; Binds the polymerase to DNA and acts as a sliding clamp; Derived by automated computational analysis using gene prediction method- Protein Homology (366 aa)
   
 
  0.777
alaS
Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (875 aa)
   
 
  0.697
xerC
Site-specific tyrosine recombinase which cuts and rejoins DNA molecules; binds cooperatively to specific DNA consensus sites; forms a heterotetrameric complex with XerC; XerCD exhibit similar sequences; essential to convert chromosome dimers to monomers during cell division and functions during plasmid segregation; cell division protein FtsK may regulate the XerCD complex; enzyme from Streptococcus group has unusual active site motifs; Derived by automated computational analysis using gene prediction method- Protein Homology (300 aa)
         
  0.645
xerD
Site-specific tyrosine recombinase which cuts and rejoins DNA molecules; binds cooperatively to specific DNA consensus sites; forms a heterotetrameric complex with XerC; XerCD exhibit similar sequences; essential to convert chromosome dimers to monomers during cell division and functions during plasmid segregation; XerD specifically exchanges the bottom strands; cell division protein FtsK may regulate the XerCD complex; enzyme from Streptococcus group has unusual active site motifs; Derived by automated computational analysis using gene prediction method- Protein Homology (298 aa)
         
  0.635
ung
Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine (229 aa)
     
 
  0.632
JG24_00085
Derived by automated computational analysis using gene prediction method- Protein Homology (775 aa)
 
 
  0.631
Your Current Organism:
Klebsiella pneumoniae
NCBI taxonomy Id: 573
Other names: ATCC 13883, Bacillus pneumoniae, Bacterium pneumoniae crouposae, CCUG 225, CIP 82.91, DSM 30104, HAMBI 450, Hyalococcus pneumoniae, IFO 14940, K. pneumoniae, Klebsiella pneumoniae, Klebsiella sp. M-AI-2, Klebsiella sp. PB12, Klebsiella sp. RCE-7, LMG 2095, NBRC 14940, NCTC 9633
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