Structure of PDB 6ait Chain D

Receptor sequence

>6aitD (length=416) Species: 83333 (Escherichia coli K-12)

SIGQEMQMGDYYVRQLRGSAPLINDPLLTQYINSLGMRLVSHANSVKTPF
HFFLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQR
HLARAMEDQTWVGALGSILLAMASPQGMISFTQQNEQEADRIGIQVLQRS
GFDPQAMPTFLEKLLDQARYSSRPPEILLTHPLPESRLADARNRANQMRP
MVVQSSEDFYLAKARTLGMYNSGRNQLTSDLLDEWAKGNVRQQRAAQYGR
ALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINR
LKNARDLRTNPVLQLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGWDL
LAQAEAALNNRDQELAARAEGYALAGRLDQAISLLSSASSQVKLGSLQQA
RYDARIDQLRQLQERF

3D structure

• PDB: 6ait Structural Basis for the Function of the beta-Barrel Assembly-Enhancing Protease BepA.
• Chain: D
• Resolution: 2.598 Å

Enzymatic activity

• Enzyme Commision number: 3.4.-.-

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	D	H136 H140 E201 H246	H92 H96 E136 H181

Gene Ontology

Molecular Function

• GO:0003756 protein disulfide isomerase activity
• GO:0004222 metalloendopeptidase activity
• GO:0005515 protein binding
• GO:0008233 peptidase activity
• GO:0008237 metallopeptidase activity
• GO:0008270 zinc ion binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006508 proteolysis
• GO:0043165 Gram-negative-bacterium-type cell outer membrane assembly
• GO:0051603 proteolysis involved in protein catabolic process
• GO:0061077 chaperone-mediated protein folding

Cellular Component

• GO:0016020 membrane
• GO:0030288 outer membrane-bounded periplasmic space
• GO:0042597 periplasmic space

External links

• PDB: RCSB:6ait, PDBe:6ait, PDBj:6ait
• PDBsum: 6ait
• PubMed: 30521812
• UniProt: P66948|BEPA_ECOLI Beta-barrel assembly-enhancing protease (Gene Name=bepA)