STRINGSTRING
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
murGUDP-N-acetylglucosamine:LPS N-acetylglucosamine 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. (354 aa)    
Predicted Functional Partners:
murC
murC: UDP-N-acetylmuramate--alanine ligase; Cell wall formation; Belongs to the MurCDEF family.
  
 0.999
mraY
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.
 
 
 0.998
murD
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.
 
  
 0.996
murF
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.
 
  
 0.992
AHY46784.1
COG:COG0772: Bacterial cell division membrane protein [Cell division and chromosome partitioning]; Pfam:PF01098:Cell cycle protein FtsW/RodA; Pfam:PF01098:Cell cycle protein FtsW/RodA; Belongs to the SEDS family.
  
 0.989
AHY46781.1
POTRA domain, FtsQ-type; COG:COG1589: Cell division septal protein [Cell envelope biogenesis outer membrane]; Pfam:PF08478:Polypeptide-transport-associated, FtsQ-type.
  
  
 0.974
AHY46788.1
COG:COG0768: Cell division protein FtsI/penicillin-binding protein 2 [Cell envelope biogenesis outer membrane]; Pfam:PF00905:Penicillin-binding protein, transpeptidase; Pfam:PF00905:Penicillin-binding protein, transpeptidase; SUPERFAMILY:SSF56601:Beta-lactamase/transpeptidase-like.
 
  
 0.968
AHY46816.1
COG:COG0769: UDP-N-acetylmuramyl tripeptide synthase [Cell envelope biogenesis outer membrane]; Pfam:PF08353:Domain of unknown function DUF1727; Pfam:PF08353:Domain of unknown function DUF1727; SUPERFAMILY:SSF53623:Mur ligase, central.
 
 0.956
ftsZ
ftsZ: cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
 
 0.954
ddl-2
D-alanine--D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family.
 
  
 0.941
Your Current Organism:
Rubrobacter radiotolerans
NCBI taxonomy Id: 42256
Other names: ATCC 51242, Arthrobacter radiotolerans, CIP 106991, DSM 46359, DSM 5868, IAM 12072, IFO 14777, JCM 2153, NBRC 14777, R. radiotolerans, strain P-1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.