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htpX protein (Gallibacterium anatis) - STRING interaction network
"htpX" - Heat shock protein HtpX in Gallibacterium anatis
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query proteins and first shell of interactors
white nodes:
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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Cooccurence
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[Homology]
Score
htpXHeat shock protein HtpX (287 aa)    
Predicted Functional Partners:
hslU
ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis (444 aa)
   
   
  0.689
pyrF
Orotidine 5’-phosphate decarboxylase; Catalyzes the decarboxylation of orotidine 5’- monophosphate (OMP) to uridine 5’-monophosphate (UMP) (231 aa)
         
  0.647
htpG
Heat shock protein 90; Molecular chaperone. Has ATPase activity (628 aa)
     
   
  0.637
UMN179_00262
Hypothetical protein (178 aa)
              0.632
prfB
Peptide chain release factor 2; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (351 aa)
     
   
  0.613
ftsH
ATP-dependent metalloprotease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (638 aa)
     
 
  0.596
dinB
DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3’-5’ exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (354 aa)
   
        0.596
dnaK
Molecular chaperone DnaK; Acts as a chaperone (639 aa)
   
 
  0.582
groS
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (96 aa)
   
   
  0.540
rne
Ribonuclease E; Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs (996 aa)
           
  0.518
Your Current Organism:
Gallibacterium anatis
NCBI taxonomy Id: 1005058
Other names: G. anatis, G. anatis UMN179, Gallibacterium, Gallibacterium Christensen et al. 2003 emend. Bisgaard et al. 2009, Gallibacterium anatis, Gallibacterium anatis UMN179, Gallibacterium anatis str. UMN179, Gallibacterium anatis strain UMN179, Pasteurella anatis, Salpingitia sp. 10672/6, Salpingitia sp. 10672/9, Salpingitia sp. 12158, Salpingitia sp. 20558, Salpingitia sp. 36961/sv7, Salpingitia sp. BJ3453, Salpingitia sp. BK3387.2, Salpingitia sp. CCM 5995, Salpingitia sp. Gerl.220, Salpingitia sp. Gerl.3348/80, Salpingitia sp. Gerl.4224, Salpingitia sp. IPDH 697/78, avian Pasteurella haemolytica complex
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