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dnaX protein (Acinetobacter baumannii) - STRING interaction network
"dnaX" - DNA polymerase III subunit gamma/tau in Acinetobacter baumannii
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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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[Homology]
Score
dnaXDNA polymerase III subunit gamma/tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity (726 aa)    
Predicted Functional Partners:
holA
DNA polymerase III, delta subunit; Derived by automated computational analysis using gene prediction method- Protein Homology (329 aa)
 
 
  0.986
AIL77614.1
DNA-directed DNA polymerase; Derived by automated computational analysis using gene prediction method- Protein Homology (1187 aa)
 
 
  0.985
AIL79765.1
Beta sliding clamp; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3’-5’ exonuclease proofreading activity. The beta chain is required for initiation of replication as [...] (382 aa)
 
 
  0.984
AIL77504.1
DNA polymerase III subunit delta; Derived by automated computational analysis using gene prediction method- Protein Homology (326 aa)
 
 
0.980
metG
methionine--tRNA ligase; MetRS; adds methionine to tRNA(Met) with cleavage of ATP to AMP and diphosphate; some MetRS enzymes form dimers depending on a C-terminal domain that is also found in other proteins such as Trbp111 in Aquifex aeolicus and the cold-shock protein CsaA from Bacillus subtilis while others do not; four subfamilies exist based on sequence motifs and zinc content; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family (687 aa)
   
   
  0.851
dnaQ
Ribonuclease H; Endonuclease that specifically degrades the RNA of RNA- DNA hybrids (459 aa)
 
  0.844
AIL80356.1
DNA polymerase I; Has 3’-5’ exonuclease, 5’-3’ exonuclease and 5’-3’polymerase activities, primarily functions to fill gaps during DNA replication and repair; Derived by automated computational analysis using gene prediction method- Protein Homology (923 aa)
 
   
  0.787
rpoD
RNA polymerase sigma factor RpoD; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth (628 aa)
 
   
  0.774
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] (370 aa)
 
 
  0.762
dnaG
DNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication; Belongs to the DnaG primase family (621 aa)
 
   
  0.757
Your Current Organism:
Acinetobacter baumannii
NCBI taxonomy Id: 470
Other names: A. baumannii, ATCC 19606, Acinetobacter baumannii, Acinetobacter genomosp. 2, Acinetobacter genomospecies 2, Bacterium anitratum, CCUG 19096, CIP 70.34, DSM 30007, JCM 6841, NCCB 85021, NCTC 12156
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