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Mfla_2210 protein (Methylobacillus flagellatus) - STRING interaction network
"Mfla_2210" - Integral membrane protein MviN in Methylobacillus flagellatus
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Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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Mfla_2210Integral membrane protein MviN; Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane (513 aa)    
Predicted Functional Partners:
Mfla_2209
Riboflavin kinase / FMN adenylyltransferase (306 aa)
 
        0.952
ileS
isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as ’pretransfer’ editing and involves the hydrolysis of activated Val-AMP. The other activity is designated ’posttransfer’ editing and involves deacylation of mischarged Val-tRNA(Ile) (934 aa)
          0.949
lspA
Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins (151 aa)
   
      0.832
rpsT
30S ribosomal protein S20; Binds directly to 16S ribosomal RNA (87 aa)
         
  0.743
glnD
PII uridylyl-transferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism (856 aa)
 
     
  0.721
pcnB
poly(A) polymerase; Adds poly(A) tail to the 3’ end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control (452 aa)
 
        0.628
mraY
phospho-N-acetylmuramoyl-pentapeptide- transferase; First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan (361 aa)
 
 
  0.615
ftsW
Cell cycle protein; Essential cell division protein. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane (392 aa)
   
   
  0.563
cca
Metal dependent phosphohydrolase; Catalyzes the addition and repair of the essential 3’- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2’- nucleotidase and 2’,3’-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3’-CCA terminus degraded by intracellular RNases (411 aa)
 
        0.553
rnpA
Ribonuclease P; RNaseP catalyzes the removal of the 5’-leader sequence from pre-tRNA to produce the mature 5’-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5’-leader sequence and broadening the substrate specificity of the ribozyme (127 aa)
   
        0.536
Your Current Organism:
Methylobacillus flagellatus
NCBI taxonomy Id: 265072
Other names: M. flagellatus, M. flagellatus KT, Methylobacillus, Methylobacillus flagellatus, Methylobacillus flagellatus KT, Methylobacillus flagellatus str. KT, Methylobacillus flagellatus strain KT
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