ID PEPT_STAAM Reviewed; 408 AA. AC P65805; Q99VN1; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=Peptidase T {ECO:0000255|HAMAP-Rule:MF_00550}; DE EC=3.4.11.4 {ECO:0000255|HAMAP-Rule:MF_00550}; DE AltName: Full=Aminotripeptidase {ECO:0000255|HAMAP-Rule:MF_00550}; DE Short=Tripeptidase {ECO:0000255|HAMAP-Rule:MF_00550}; DE AltName: Full=Tripeptide aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00550}; GN Name=pepT {ECO:0000255|HAMAP-Rule:MF_00550}; GN OrderedLocusNames=SAV0743; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu50 / ATCC 700699; RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., RA Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; RL Lancet 357:1225-1240(2001). CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides. CC {ECO:0000255|HAMAP-Rule:MF_00550}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of the N-terminal residue from a tripeptide.; CC EC=3.4.11.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00550}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00550}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00550}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00550}. CC -!- SIMILARITY: Belongs to the peptidase M20B family. {ECO:0000255|HAMAP- CC Rule:MF_00550}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000017; BAB56905.1; -; Genomic_DNA. DR RefSeq; WP_000795811.1; NC_002758.2. DR AlphaFoldDB; P65805; -. DR SMR; P65805; -. DR MEROPS; M20.003; -. DR KEGG; sav:SAV0743; -. DR HOGENOM; CLU_053676_0_0_9; -. DR PhylomeDB; P65805; -. DR Proteomes; UP000002481; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule. DR CDD; cd03892; M20_peptT; 1. DR Gene3D; 3.30.70.360; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR HAMAP; MF_00550; Aminopeptidase_M20; 1. DR InterPro; IPR001261; ArgE/DapE_CS. DR InterPro; IPR036264; Bact_exopeptidase_dim_dom. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR InterPro; IPR010161; Peptidase_M20B. DR NCBIfam; TIGR01882; peptidase-T; 1. DR PANTHER; PTHR42994; PEPTIDASE T; 1. DR PANTHER; PTHR42994:SF1; PEPTIDASE T; 1. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF037215; Peptidase_M20B; 1. DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1. DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1. DR World-2DPAGE; 0002:P65805; -. PE 3: Inferred from homology; KW Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; KW Protease; Zinc. FT CHAIN 1..408 FT /note="Peptidase T" FT /id="PRO_0000185316" FT ACT_SITE 80 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT ACT_SITE 174 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 175 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 197 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" FT BINDING 379 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550" SQ SEQUENCE 408 AA; 45820 MW; 28A88DC436056671 CRC64; MKNQLIDRLT RYTTIDTQSD PKSTTTPSTE KQWDLLHLLE KELQQLGLPT DLDENGYLFA TLESNIDADV PTVGFLAHVD TSPDFNASNV KPQIIENYDG KPYKLGNTKR VLDPKVFPEL NSLVGHTLMV TDGTSLLGAD DKAGIVEIME AICYLQEHPE IKHGTIRIGF TPDEEIGRGP HKFDVDRFNA DFAYTMDGSQ YGELQYESFN AAEAVITCHG VNVHPGSAKN AMVNAIRLGE QFDSLLPDSE VPERTEGYEG FYHLMNFEGT VEKATLQYII RDHDKKQFEL RKKRILEIRD DINAHFENYP VKVDISDQYF NMAEKILPLP HIIDIPKRVF AKLDIPANTE PIRGGTDGSQ LSFMGLPTPN IFTGCGNFHG PYEYASIDVM EKAVQVIIGI VEDIAENH //