| 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 |