Function and Biology Details
Reaction catalysed:
ATP-dependent cleavage of peptide bonds with broad specificity.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero 24-mer (preferred)
Assembly name:
AAA+ proteases (preferred)
PDBe Complex ID:
PDB-CPX-155128 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent protease ATPase subunit HslU
Molecule details ›
Chains: A, B, C, D, E, F, S, T, U, V, W, X
Length: 444 amino acids
Theoretical weight: 49.44 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains:
Length: 444 amino acids
Theoretical weight: 49.44 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P43773 (Residues: 1-444; Coverage: 100%)
Sequence domains:
Structure domains:
ATP-dependent protease subunit HslV
Molecule details ›
Chains: G, H, I, J, K, L, M, N, O, P, Q, R
Length: 174 amino acids
Theoretical weight: 18.9 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Proteasome subunit
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Length: 174 amino acids
Theoretical weight: 18.9 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P43772 (Residues: 2-175; Coverage: 99%)
Sequence domains: Proteasome subunit
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
