Function and Biology Details
Reactions catalysed:
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidase M24, methionine aminopeptidase
- Peptidase M24A, methionine aminopeptidase, subfamily 1
- Trigger factor
- Creatinase/aminopeptidase-like
- Trigger factor, C-terminal
- Trigger factor, C-terminal domain superfamily
- Trigger factor/SurA domain superfamily
- Transcription elongation factor GreA/GreB, C-terminal domain superfamily
3 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Methionine aminopeptidase and Trigger factor (preferred)
PDBe Complex ID:
PDB-CPX-142399 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Methionine aminopeptidase
Molecule details ›
Chain: P
Length: 264 amino acids
Theoretical weight: 29.34 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
Sequence domains: Metallopeptidase family M24
Length: 264 amino acids
Theoretical weight: 29.34 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
- Canonical:
P0AE18 (Residues: 1-264; Coverage: 100%)
Sequence domains: Metallopeptidase family M24
Trigger factor
Molecule details ›
Chain: Q
Length: 406 amino acids
Theoretical weight: 47.96 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 406 amino acids
Theoretical weight: 47.96 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q9WZF8 (Residues: 1-405; Coverage: 95%)
Sequence domains:
