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hda protein (Klebsiella pneumoniae) - STRING interaction network
"hda" - DnaA regulatory inactivator Hda 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
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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hdaDnaA regulatory inactivator Hda; Mediates the interaction of DNA replication inititator protein DnaA with DNA polymerase subunit beta sliding clamp (dnaN). Stimulates hydrolysis of ATP-DnaA to ADP-DnaA, rendering DnaA inactive for reinititation, a process called regulatory inhibition of DnaA or RIDA (225 aa)    
Predicted Functional Partners:
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)
 
 
  0.965
upp
Uracil phosphoribosyltransferase; Catalyzes the conversion of uracil and 5-phospho-alpha- D-ribose 1-diphosphate (PRPP) to UMP and diphosphate (208 aa)
 
   
  0.881
JG24_18630
Uracil permease; Derived by automated computational analysis using gene prediction method- Protein Homology (428 aa)
 
   
  0.840
JG24_09665
Enoyl-[acyl-carrier-protein] reductase [NADH]; Catalyzes a key regulatory step in fatty acid biosynthesis; Derived by automated computational analysis using gene prediction method- Protein Homology (262 aa)
         
  0.727
dnaA
Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box)- 5’-TTATC[CA]A[CA]A-3’. DnaA binds to ATP and to acidic phospholipids (467 aa)
   
 
0.727
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
   
   
  0.668
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 [...] (673 aa)
   
   
  0.642
JG24_27195
Replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins (471 aa)
   
 
  0.608
JG24_29705
Has polymerase, DNA-binding and 3’-5’ exonuclease activities. In Aeropyrum pernix this protein is sensitive to aphidicolin and stable at 95#C; Derived by automated computational analysis using gene prediction method- Protein Homology (785 aa)
           
  0.600
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)
 
     
  0.599
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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