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Mettu_1839 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_1839" - Peptidase S16 lon domain protein in Methylobacter tundripaludum
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second shell of interactors
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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
Mettu_1839Peptidase S16 lon domain protein (797 aa)    
Predicted Functional Partners:
rlmL
Ribosomal RNA large subunit methyltransferase K/L ; Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA (774 aa)
     
      0.575
Mettu_3874
ATP-dependent Clp protease ATP-binding subunit ClpX ; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (424 aa)
         
  0.553
Mettu_0228
ATP-dependent protease La ; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (806 aa)
         
  0.552
mnmA
tRNA-specific 2-thiouridylase MnmA ; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34 (363 aa)
   
        0.548
Mettu_3381
ATP-dependent Clp protease ATP-binding subunit ClpX ; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (423 aa)
         
  0.525
Mettu_3873
ATP-dependent protease La ; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (810 aa)
         
0.517
Mettu_1304
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 (463 aa)
   
        0.511
fabA
Trans-2-decenoyl-[acyl-carrier-protein] isomerase ; Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl- ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)- decenoyl-ACP. Can catalyze the dehydratase reaction for beta- hydroxyacyl-ACPs with saturated chain lengths up to 16-0, being most active on intermediate chain length (171 aa)
   
        0.499
Mettu_0073
tRNA methyl transferase-like protein (348 aa)
   
        0.494
rplI
50S ribosomal protein L9 ; Binds to the 23S rRNA (149 aa)
              0.493
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
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