Function and Biology Details
Reaction catalysed:
n UDP-N-acetyl-alpha-D-glucosamine + 4-O-(D-ribitylphospho)(n)-di((2R)-1-glycerophospho)-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-(2-N-acetyl-alpha-D-glucosaminyl-D-ribitylphospho)(n)-di((2R)-1-glycerophospho)-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Biochemical function:
Biological process:
Cellular component:
Sequence domain:
Structure analysis Details
Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101610 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase
Molecule details ›
Chains: A, B, C, D
Length: 493 amino acids
Theoretical weight: 57.36 KDa
Source organism: Staphylococcus aureus subsp. aureus 21178
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Glycosyl transferases group 1
Structure domains: Glycogen Phosphorylase B;
Length: 493 amino acids
Theoretical weight: 57.36 KDa
Source organism: Staphylococcus aureus subsp. aureus 21178
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A0A0H2WWV6 (Residues: 1-493; Coverage: 100%)
Sequence domains: Glycosyl transferases group 1
Structure domains: Glycogen Phosphorylase B;
