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HX89_08070 protein (Dermacoccus nishinomiyaensis) - STRING interaction network
"HX89_08070" - Uncharacterized protein in Dermacoccus nishinomiyaensis
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
HX89_08070Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology (290 aa)    
Predicted Functional Partners:
HX89_08080
Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology (504 aa)
         
  0.542
HX89_08075
Uncharacterized protein; Derived by automated computational analysis using gene prediction method- GeneMarkS+ (155 aa)
              0.530
dnaK
Chaperone protein DnaK; Acts as a chaperone (628 aa)
   
 
  0.512
HX89_12810
Crp/Fnr family transcriptional regulator; Derived by automated computational analysis using gene prediction method- Protein Homology (225 aa)
     
 
  0.486
HX89_08085
Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology (621 aa)
         
  0.484
alaS
Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (904 aa)
   
 
  0.464
HX89_09740
Nitrogen regulatory protein P-II 1; Indirectly regulates nitrogen metabolism; at high nitrogen levels P-II prevents the phosphorylation of NR-I, the transcriptional activator of the glutamine synthetase gene (glnA); at low nitrogen levels P-II is uridylylated to form PII-UMP and interacts with an adenylyltransferase (GlnE) that activates GlnA; Derived by automated computational analysis using gene prediction method- Protein Homology (112 aa)
       
 
  0.460
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 [...] (377 aa)
     
 
  0.443
HX89_03070
Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method- Protein Homology (337 aa)
     
 
  0.443
rpoC
DNA-directed RNA polymerase subunit beta’; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (1298 aa)
     
 
  0.437
Your Current Organism:
Dermacoccus nishinomiyaensis
NCBI taxonomy Id: 1274
Other names: ATCC 29093, CCM 2140, CCUG 33028, CIP 81.71, D. nishinomiyaensis, DSM 20448, Dermacoccus nishinomiyaensis, Dermacoccus nishinomiyensis, Dermatococcus nishinomiyaensis, Dermatococcus nishinomiyensis, IEGM 393, IFO 15356, JCM 11613, LMG 14222, Micrococcus nishinomiyaensis, Micrococcus nishinomyaensis, NBRC 15356, NCTC 11039
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