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JG24_19700 protein (Klebsiella pneumoniae) - STRING interaction network
"JG24_19700" - C-terminal domain of CinA type S Protein Implicated in DNA repair function with RecA and MutS in Klebsiella pneumoniae
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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JG24_19700C-terminal domain of CinA type S Protein Implicated in DNA repair function with RecA and MutS; Derived by automated computational analysis using gene prediction method- Protein Homology (165 aa)    
Predicted Functional Partners:
JG24_05775
Derived by automated computational analysis using gene prediction method- Protein Homology (216 aa)
 
 
  0.944
JG24_17725
Molybdopterin binding motif, CinA N-terminal domain / C-terminal domain of CinA type E; Derived by automated computational analysis using gene prediction method- Protein Homology (398 aa)
     
  0.926
pncB
Nicotinate phosphoribosyltransferase; Catalyzes the synthesis of beta-nicotinate D- ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP (400 aa)
   
 
  0.922
JG24_29985
Quinolinate phosphoribosyltransferase [decarboxylating]; Catalyzes the formation of pyridine-2,3-dicarboxylate and 5-phospho-alpha-D-ribose 1-diphosphate from nictinate D-ribonucleotide; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the NadC/ModD family (297 aa)
   
 
  0.919
JG24_29350
Catalyzes the formation of NAD(+) from nicotinamide ribonucleotide; catalyzes the formation of nicotinamide mononucleotide from nicotinamide riboside; also has a regulatory function; Derived by automated computational analysis using gene prediction method- Protein Homology (410 aa)
   
 
    0.917
surE
5’/3’-nucleotidase SurE; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5’- monophosphates and ribonucleoside 3’-monophosphates with highest affinity to 3’-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain- length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3’-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs (253 aa)
   
 
    0.903
JG24_29280
Manganese-dependent 5’-nucleotidase; specific for 5’-UMP, 5’-dUMP, and 5’-dTMP; member of haloacid dehalogenase (HAD)-like hydrolase superfamily; Derived by automated computational analysis using gene prediction method- Protein Homology (225 aa)
   
 
    0.902
nudC
NADH pyrophosphatase; Can catalyze hydrolysis of broad range of dinucleotide pyrophosphates but prefers reduced form of NADH; requires divalent metal ions such as magnesium and manganese and produces two mononucleoside 5’-phosphates; Derived by automated computational analysis using gene prediction method- Protein Homology (257 aa)
     
 
    0.902
JG24_23760
FIG001957- putative hydrolase; Derived by automated computational analysis using gene prediction method- Protein Homology (227 aa)
       
    0.901
mazG
Nucleoside triphosphate pyrophosphohydrolase MazG; Functions in degradation of stringent response intracellular messenger ppGpp; in Escherichia coli this gene is co-transcribed with the toxin/antitoxin genes mazEF; activity of MazG is inhibited by MazEF in vitro; ppGpp inhibits mazEF expression; MazG thus works in limiting the toxic activity of the MazF toxin induced during starvation; MazG also interacts with the GTPase protein Era; Derived by automated computational analysis using gene prediction method- Protein Homology (263 aa)
         
    0.900
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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