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STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
murCUDP-N-acetylmuramate--L-alanine ligase; Cell wall formation; Belongs to the MurCDEF family. (461 aa)    
Predicted Functional Partners:
murB
UDP-N-acetylmuramate dehydrogenase; Cell wall formation.
 
 0.999
murG
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily.
  
 0.998
murD
UDP-N-acetylmuramoylalanine--D-glutamate ligase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family.
 
 
0.995
ddl
D-alanine--D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family.
  
 0.976
Toce_0955
Polypeptide-transport-associated domain protein FtsQ-type; Essential cell division protein.
  
  
 0.968
murA
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily.
 
  
 0.965
mraY
Phospho-N-acetylmuramoyl-pentapeptide- transferase; First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan; Belongs to the glycosyltransferase 4 family. MraY subfamily.
 
  
 0.963
glmU
Glucosamine-1-phosphate N-acetyltransferase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain.
    
 0.959
murF
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D- alanine ligase; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein; Belongs to the MurCDEF family. MurF subfamily.
 
  
0.952
Toce_0946
COGs: COG0768 Cell division protein FtsI/penicillin-binding protein 2; InterPro IPR005543:IPR005311:IPR001460:IPR011927; KEGG: hor:Hore_09030 stage V sporulation protein D; PFAM: penicillin-binding protein transpeptidase; Penicillin-binding protein dimerisation domain; PASTA domain containing protein; PRIAM: Peptidoglycan glycosyltransferase; SMART: PASTA domain containing protein; SPTR: Stage V sporulation protein D; TIGRFAM: stage V sporulation protein D; PFAM: Penicillin binding protein transpeptidase domain; Penicillin-binding Protein dimerisation domain; PASTA domain; TIGRFAM: sta [...]
 
 
 0.923
Your Current Organism:
Thermosediminibacter oceani
NCBI taxonomy Id: 555079
Other names: T. oceani DSM 16646, Thermosediminibacter oceani DSM 16646, Thermosediminibacter oceani JW/IW-1228P, Thermosediminibacter oceani str. DSM 16646, Thermosediminibacter oceani strain DSM 16646
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