Function and Biology Details
Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- DNA-directed RNA polymerase, phage-type
- N-acetylmuramoyl-L-alanine amidase domain
- DNA-directed RNA polymerase, N-terminal
- N-acetylmuramoyl-L-alanine amidase/PGRP domain superfamily
- DNA-directed RNA polymerase, C-terminal domain, phage-type
- DNA-directed RNA polymerase, helix hairpin domain superfamily
- DNA-directed RNA polymerase, N-terminal domain superfamily
- DNA/RNA polymerase superfamily
3 more domains
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Endolysin and T7 RNA polymerase (preferred)
PDBe Complex ID:
PDB-CPX-132726 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
T7 RNA polymerase
Molecule details ›
Chain: P
Length: 883 amino acids
Theoretical weight: 98.94 KDa
Source organism: Escherichia phage T7
Expression system: Escherichia coli BL21
UniProt:
Sequence domains:
Structure domains:
Length: 883 amino acids
Theoretical weight: 98.94 KDa
Source organism: Escherichia phage T7
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P00573 (Residues: 1-883; Coverage: 100%)
Sequence domains:
Structure domains:
Endolysin
Molecule details ›
Chain: L
Length: 151 amino acids
Theoretical weight: 17.01 KDa
Source organism: Escherichia phage T7
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Peptidoglycan recognition protein-like
Length: 151 amino acids
Theoretical weight: 17.01 KDa
Source organism: Escherichia phage T7
Expression system: Escherichia coli BL21
UniProt:
- Canonical: P00806 (Residues: 1-151; Coverage: 100%)
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Peptidoglycan recognition protein-like
