Detail Information for IndEnz0002018538
IED ID IndEnz0002018538
Enzyme Type ID protease018538
Protein Name Beta-barrel assembly-enhancing protease
EC 3.4.-.-
Gene Name bepA yfgC b2494 JW2479
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MFRQLKKNLVATLIAAMTIGQVAPAFADSADTLPDMGTSAGSTLSIGQEMQMGDYYVRQLRGSAPLINDPLLTQYINSLGMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEDQQRSAPLTWVGALGSILLAMASPQAGMAALTGTLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPTFLEKLLDQARYSSRPPEILLTHPLPESRLADARNRANQMRPMVVQSSEDFYLAKARTLGMYNSGRNQLTSDLLDEWAKGNVRQQRAAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLRTNPVLQLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAARAEGYALAGRLDQAISLLSSASSQVKLGSLQQARYDARIDQLRQLQERFKPYTKM
Enzyme Length 487
Uniprot Accession Number P66948
Absorption
Active Site ACT_SITE 137; /evidence=ECO:0000255|HAMAP-Rule:MF_00997; ACT_SITE 205; /note=Proton donor; /evidence=ECO:0000255|HAMAP-Rule:MF_00997
Activity Regulation ACTIVITY REGULATION: Protease activity is inhibited by the metal chelating reagents 1,10-phenanthroline and EDTA. {ECO:0000269|PubMed:24003122}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.-.-
Enzyme Function FUNCTION: Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions. {ECO:0000255|HAMAP-Rule:MF_00997, ECO:0000269|PubMed:22491786, ECO:0000269|PubMed:24003122}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (3); Chain (1); Helix (23); Metal binding (3); Mutagenesis (2); Repeat (4); Signal peptide (1); Turn (2)
Keywords 3D-structure;Hydrolase;Metal-binding;Metalloprotease;Periplasm;Protease;Reference proteome;Repeat;Signal;TPR repeat;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00997, ECO:0000269|PubMed:22491786, ECO:0000269|PubMed:24003122}. Note=A significant amount of BepA is membrane-associated. This localization could result from interaction with the BAM complex.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..27; /evidence=ECO:0000255|HAMAP-Rule:MF_00997
Structure 3D X-ray crystallography (3)
Cross Reference PDB 5XI8; 6AIT; 6SAR;
Mapped Pubmed ID 15690043; 16606699; 20487295; 28960545; 30521812; 33106348;
Motif
Gene Encoded By
Mass 53,908
Kinetics
Metal Binding METAL 136; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_00997; METAL 140; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_00997; METAL 201; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_00997
Rhea ID
Cross Reference Brenda