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
anmKProtein of unknown function UPF0075; 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; Belongs to the anhydro-N-acetylmuramic acid kinase family. (375 aa)    
Predicted Functional Partners:
ACS21278.1
PFAM: Peptidase M23; KEGG: ajs:Ajs_0631 peptidase M23B.
 
    0.837
nagZ
Glycoside hydrolase family 3 domain protein; Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide- linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N- acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
 
   
 0.630
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); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily.
       0.607
ACS17608.1
N-acetylmuramyl-L-alanine amidase, negative regulator of AmpC, AmpD; PFAM: N-acetylmuramoyl-L-alanine amidase family 2; SMART: N-acetylmuramoyl-L-alanine amidase family 2; KEGG: pol:Bpro_1109 N-acetyl-anhydromuranmyl-L-alanine amidase.
  
   
 0.517
ACS19727.1
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
     
 0.513
mltG
Aminodeoxychorismate lyase; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
 
   
 0.490
ACS21878.1
PFAM: aminoglycoside phosphotransferase; KEGG: rfr:Rfer_0099 aminoglycoside phosphotransferase.
 
   
 0.476
gcvP
Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
      
 0.422
uvrC
Excinuclease ABC, C subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
  
   
 0.417
ACS19418.1
PFAM: peptidase U61 LD-carboxypeptidase A; KEGG: pol:Bpro_2448 muramoyltetrapeptide carboxypeptidase.
 
   
 0.408
Your Current Organism:
Variovorax paradoxus S110
NCBI taxonomy Id: 543728
Other names: V. paradoxus S110, Variovorax paradoxus str. S110, Variovorax paradoxus strain S110
Server load: medium (50%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.