STRINGSTRING
ligA protein (Staphylococcus xylosus) - STRING interaction network
"ligA" - DNA ligase in Staphylococcus xylosus
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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
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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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ligADNA ligase; DNA ligase that catalyzes the formation of phosphodiester linkages between 5’-phosphoryl and 3’-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA; Belongs to the NAD-dependent DNA ligase family. LigA subfamily (667 aa)    
Predicted Functional Partners:
AID42354.1
annotation not available (736 aa)
 
 
  0.961
pcrB
Heptaprenylglyceryl phosphate synthase; Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales (230 aa)
              0.901
AID42356.1
Uncharacterized protein; Homology with cAM373 (402 aa)
         
  0.890
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (876 aa)
 
   
  0.794
uvrB
UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...] (660 aa)
 
 
  0.771
gyrA
DNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner (904 aa)
   
   
  0.767
AID41438.1
DNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner (641 aa)
   
 
  0.754
AID42591.1
annotation not available (759 aa)
 
   
  0.729
AID43087.1
annotation not available (570 aa)
 
   
  0.727
AID42344.1
annotation not available (267 aa)
         
  0.709
Your Current Organism:
Staphylococcus xylosus
NCBI taxonomy Id: 1288
Other names: ATCC 29971, CCUG 7324, CIP 81.66, DSM 20266, HAMBI 2057, JCM 2418, NCTC 11043, NRRL B-14776, S. xylosus, Staphylococcus xylosus
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