STRINGSTRING
Mettu_3060 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_3060" - Heat shock protein HtpX in Methylobacter tundripaludum
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
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
Edges:
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
Mettu_3060Heat shock protein HtpX (292 aa)    
Predicted Functional Partners:
Mettu_3062
Putative uncharacterized protein (44 aa)
              0.779
Mettu_3061
Putative uncharacterized protein (129 aa)
              0.779
hslU
Unfoldase 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 (439 aa)
     
   
  0.725
Mettu_4282
Isoprenylcysteine carboxyl methyltransferase (190 aa)
     
  0.693
Mettu_3204
ATP-dependent zinc metalloprotease FtsH ; 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 (647 aa)
     
 
  0.669
pyrF
OMP decarboxylase ; Catalyzes the decarboxylation of orotidine 5’- monophosphate (OMP) to uridine 5’-monophosphate (UMP) (241 aa)
         
  0.648
htpG
High temperature protein G ; Molecular chaperone. Has ATPase activity (642 aa)
     
   
  0.636
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 (365 aa)
     
   
  0.634
dnaK
Heat shock protein 70 ; Acts as a chaperone (644 aa)
   
 
  0.626
groS
Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (95 aa)
   
   
  0.612
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
Server load: low (8%) [HD]