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Mettu_3558 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_3558" - Peptidase M23 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_3558Peptidase M23 (490 aa)    
Predicted Functional Partners:
anmK
AnhMurNAc kinase ; Catalyzes the specific phosphorylation of 1,6-anhydro-N- acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling (385 aa)
         
  0.918
tyrS
Tyrosyl-tRNA synthetase ; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) (398 aa)
              0.768
Mettu_2412
Carboxyl-terminal protease (437 aa)
 
 
  0.759
Mettu_2411
Peptidase M23 (407 aa)
   
          0.756
Mettu_1092
Penicillin-binding protein, 1A family (781 aa)
   
     
  0.665
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)
     
   
  0.635
Mettu_4341
Pyruvate kinase (484 aa)
           
  0.631
Mettu_2431
Pyruvate kinase (481 aa)
           
  0.631
Mettu_0149
Cell division protein FtsX ; Part of the ABC transporter FtsEX involved in cellular division (332 aa)
 
 
      0.626
atpH
F-type ATPase subunit delta ; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (176 aa)
       
      0.621
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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