AC MF_00550; DC Protein; auto TR HAMAP; MF_00550; -; 1; level=0 XX Names: Aminopeptidase_M20 XX ID PEPT DE RecName: Full=Peptidase T; DE EC=3.4.11.4; DE AltName: Full=Aminotripeptidase; DE Short=Tripeptidase; DE AltName: Full=Tripeptide aminopeptidase; GN Name=pepT; XX CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of the N-terminal residue from a tripeptide.; CC EC=3.4.11.4; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ions per subunit.; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the peptidase M20B family. XX DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1; trigger=no DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1; trigger=no DR Pfam; PF07687; M20_dimer; 1; trigger=no DR Pfam; PF01546; Peptidase_M20; 1; trigger=no DR NCBIfam; TIGR01882; Peptidase-T; 1; trigger=no XX KW Cytoplasm KW Hydrolase KW Protease KW Aminopeptidase KW Metalloprotease KW Metal-binding KW Zinc XX GO GO:0045148; F:tripeptide aminopeptidase activity GO GO:0008270; F:zinc ion binding GO GO:0006508; P:proteolysis GO GO:0043171; P:peptide catabolic process GO GO:0005737; C:cytoplasm XX FT From: PEPT_SALTY (P26311) FT ACT_SITE 80 FT Condition: D FT ACT_SITE 173 FT /note="Proton acceptor" FT Condition: E FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: H FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: D FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: D FT BINDING 174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: E FT BINDING 196 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: D FT BINDING 379 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: H XX Size: 406-413; Related: None; Template: P26311; P55179; P29745; P0C2T7; Q9L4G1; P81207; Q76HM7; Q76HM5; Q84BV2; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.35 2023/06/01 //