AC MF_00997; DC Protein; auto TR HAMAP; MF_00997; -; 1; level=0 XX Names: Protease_BepA XX ID BEPA case DE RecName: Full=Beta-barrel assembly-enhancing protease; DE EC=3.4.-.-; GN Name=bepA; else DE RecName: Full=Putative beta-barrel assembly-enhancing protease; DE EC=3.4.-.-; end case XX CC -!- FUNCTION: Functions as both a chaperone and a metalloprotease. CC Maintains the integrity of the outer membrane by promoting either the CC assembly or the elimination of outer membrane proteins, depending on CC their folding state. case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; end case CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the peptidase M48 family. BepA subfamily. XX DR PROSITE; PS50005; TPR; 1; trigger=no DR PROSITE; PS50293; TPR_REGION; 1; trigger=no DR Pfam; PF01435; Peptidase_M48; 1; trigger=no DR Pfam; PF07720; TPR_3; 1; trigger=no DR Pfam; PF07719; TPR_2; 1; trigger=no DR General; Signal; -; 1; trigger=yes DR REP; Repeat_TPR; TPR; 0-6; trigger=yes XX KW Hydrolase KW Metalloprotease KW Periplasm KW Protease KW Signal case KW Metal-binding KW Zinc end case XX GO GO:0008233; F:peptidase activity case GO GO:0008270; F:zinc ion binding end case GO GO:0042597; C:periplasmic space XX FT From: BEPA_ECOLI (P66948) FT ACT_SITE 137 FT Condition: E FT ACT_SITE 205 FT /note="Proton donor" FT Condition: D FT BINDING 136 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: E XX Size: 435-600; Related: None; Template: P66948; Scope: Bacteria; Gammaproteobacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.7 2022/11/19 //