Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Nucleic acid-binding, OB-fold
- Translation elongation factor P/YeiP, central
- Translation elongation factor P
- Translation elongation factor P/YeiP
- Lysyl-tRNA synthetase, class II, C-terminal
- Elongation factor P--(R)-beta-lysine ligase
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Translation elongation factor P/YeiP, conserved site
6 more domains
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141404 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Elongation factor P--(R)-beta-lysine ligase
Molecule details ›
Chains: A, C, E, G
Length: 328 amino acids
Theoretical weight: 37.3 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: tRNA synthetases class II (D, K and N)
Structure domains: Bira Bifunctional Protein; Domain 2
Length: 328 amino acids
Theoretical weight: 37.3 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P0A8N7 (Residues: 1-325; Coverage: 100%)
Sequence domains: tRNA synthetases class II (D, K and N)
Structure domains: Bira Bifunctional Protein; Domain 2
Elongation factor P
Molecule details ›
Chains: B, D, F, H
Length: 191 amino acids
Theoretical weight: 20.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 191 amino acids
Theoretical weight: 20.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: P0A6N4 (Residues: 1-188; Coverage: 100%)
Sequence domains:
- Elongation factor P (EF-P) KOW-like domain
- Elongation factor P (EF-P) OB domain
- Elongation factor P, C-terminal
