STRINGSTRING
ligB protein (Klebsiella pneumoniae) - STRING interaction network
"ligB" - DNA ligase, LigB in Klebsiella pneumoniae
Nodes:
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ligBDNA ligase, LigB; This ligase is similar to LigA but it lacks the C-terminal BRCT domain; catalyzes strand joining of nicked DNA in the presence of a divalent cation and NAD+; Derived by automated computational analysis using gene prediction method- Protein Homology (559 aa)    
Predicted Functional Partners:
ligA
DNA 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 (671 aa)
   
 
0.880
JG24_16630
Derived by automated computational analysis using gene prediction method- Protein Homology (1171 aa)
     
 
  0.789
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
 
   
  0.730
JG24_07100
Cell division protein FtsK; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the FtsK/SpoIIIE/SftA family (1373 aa)
   
   
  0.656
secY
Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (443 aa)
     
   
  0.627
JG24_10255
Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method- Protein Homology (1175 aa)
     
 
  0.607
gmk
Guanylate kinase; Essential for recycling GMP and indirectly, cGMP (207 aa)
     
 
  0.591
recG
ATP-dependent DNA helicase RecG; Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3’- to 5’- polarity. Unwinds branched duplex DNA (Y-DNA) (693 aa)
 
   
  0.586
gyrB
DNA gyrase subunit B; Negatively supercoils closed circular double-stranded DNA; Derived by automated computational analysis using gene prediction method- Protein Homology (804 aa)
   
 
  0.586
birA
Bifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5’-adenylate (BirA-bio- 5’-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon (320 aa)
         
  0.579
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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