Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Pili assembly chaperone, bacterial
- Immunoglobulin-like fold
- Fimbrial-type adhesion domain
- Adhesion domain superfamily
- Fimbrial-type adhesion domain superfamily
- Pili assembly chaperone, C-terminal
- Pili assembly chaperone, C-terminal domain superfamily
- Pili assembly chaperone, conserved site
2 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137418 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone protein FimC
Molecule details ›
Chains: A, C
Length: 205 amino acids
Theoretical weight: 22.75 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 205 amino acids
Theoretical weight: 22.75 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P31697 (Residues: 37-241; Coverage: 100%)
Sequence domains:
- Pili and flagellar-assembly chaperone, PapD N-terminal domain
- Pili assembly chaperone PapD, C-terminal domain
Type-1 fimbrial protein, A chain
Molecule details ›
Chains: B, D
Length: 143 amino acids
Theoretical weight: 14.3 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Fimbrial protein
Length: 143 amino acids
Theoretical weight: 14.3 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P04128 (Residues: 41-182; Coverage: 89%)
Sequence domains: Fimbrial protein
