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lspA protein (Methylobacter tundripaludum) - STRING interaction network
"lspA" - Signal peptidase II in Methylobacter tundripaludum
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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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[Homology]
Score
lspASignal peptidase II ; This protein specifically catalyzes the removal of signal peptides from prolipoproteins (169 aa)    
Predicted Functional Partners:
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) (943 aa)
 
   
  0.955
lgt
Prolipoprotein diacylglyceryl transferase ; Transfers the N-acyl diglyceride group on what will become the N-terminal cysteine of membrane lipoproteins (265 aa)
 
   
  0.948
Mettu_1554
Riboflavin biosynthesis protein (327 aa)
 
        0.901
ispH
4-hydroxy-3-methylbut-2-enyl diphosphate reductase ; Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) (315 aa)
 
   
  0.891
Mettu_1137
Signal peptidase I (258 aa)
     
   
  0.839
lolA
Outer-membrane lipoprotein carrier protein ; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane) (196 aa)
     
   
  0.824
Mettu_2655
Apolipoprotein N-acyltransferase ; Transfers the fatty acyl group on membrane lipoproteins (498 aa)
   
   
  0.800
Mettu_3543
Peptidoglycan-associated lipoprotein (191 aa)
   
   
  0.713
bamA
Outer membrane protein assembly factor BamA ; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (793 aa)
 
   
  0.685
secY
Protein translocase subunit SecY ; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (440 aa)
   
   
  0.643
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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