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Mettu_0309 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_0309" - Putative uncharacterized protein in Methylobacter tundripaludum
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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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Mettu_0309Putative uncharacterized protein (381 aa)    
Predicted Functional Partners:
Mettu_0310
Putative uncharacterized protein (55 aa)
              0.636
Mettu_2356
Glutamine amidotransferase of anthranilate synthase (212 aa)
   
      0.620
Mettu_1450
Glutamine amidotransferase of anthranilate synthase (214 aa)
   
      0.620
Mettu_4090
Glycosyl transferase, family 3 (342 aa)
       
      0.612
trpD
Anthranilate phosphoribosyltransferase ; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5’-phosphoribosyl)-anthranilate (PRA) (338 aa)
       
      0.612
Mettu_2127
Transcriptional regulator, BadM/Rrf2 family (151 aa)
 
          0.501
dnaA
Chromosomal replication initiator protein DnaA ; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box)- 5’-TTATC[CA]A[CA]A-3’. DnaA binds to ATP and to acidic phospholipids (438 aa)
   
        0.499
Mettu_1208
DnaA regulatory inactivator Hda (234 aa)
   
        0.499
ispG
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase ; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (405 aa)
              0.493
alaS
Alanyl-tRNA synthetase ; 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 (870 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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