ID A0A317ZD38_STAPS Unreviewed; 407 AA. AC A0A317ZD38; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 27-MAR-2024, entry version 23. DE RecName: Full=Peptidase T {ECO:0000256|HAMAP-Rule:MF_00550}; DE EC=3.4.11.4 {ECO:0000256|HAMAP-Rule:MF_00550}; DE AltName: Full=Aminotripeptidase {ECO:0000256|HAMAP-Rule:MF_00550}; DE Short=Tripeptidase {ECO:0000256|HAMAP-Rule:MF_00550}; DE AltName: Full=Tripeptide aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00550}; GN Name=pepT {ECO:0000256|HAMAP-Rule:MF_00550, GN ECO:0000313|EMBL:PWZ99788.1}; GN ORFNames=DD924_00790 {ECO:0000313|EMBL:PWZ99788.1}, DV961_09120 GN {ECO:0000313|EMBL:REA80909.1}; OS Staphylococcus pseudintermedius. OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus; Staphylococcus intermedius group. OX NCBI_TaxID=283734 {ECO:0000313|EMBL:PWZ99788.1, ECO:0000313|Proteomes:UP000246351}; RN [1] {ECO:0000313|EMBL:PWZ99788.1, ECO:0000313|Proteomes:UP000246351} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST71 3 {ECO:0000313|EMBL:PWZ99788.1, RC ECO:0000313|Proteomes:UP000246351}; RX PubMed=29292005; DOI=10.1016/j.vetmic.2017.11.018; RA Worthing K.A., Abraham S., Coombs G.W., Pang S., Saputra S., Jordan D., RA Trott D.J., Norris J.M.; RT "Clonal diversity and geographic distribution of methicillin-resistant RT Staphylococcus pseudintermedius from Australian animals: Discovery of novel RT sequence types."; RL Vet. Microbiol. 213:58-65(2018). RN [2] {ECO:0000313|EMBL:REA80909.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ST496-2 {ECO:0000313|EMBL:REA80909.1}; RX PubMed=30173756; DOI=10.1016/j.vetmic.2018.07.021; RA Worthing K.A., Brown J., Gerber L., Abraham S., Trott D., Norris J.M.; RT "Methicillin-resistant staphylococci amongst veterinary personnel, RT personnel-owned pets, patients and the hospital environment of two small RT animal veterinary hospitals."; RL Vet. Microbiol. 223:79-85(2018). RN [3] {ECO:0000313|Proteomes:UP000256409} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST496-2 {ECO:0000313|Proteomes:UP000256409}; RA Worthing K.A., Brown J., Gerber L., Abraham S., Trott D., Norris J.M.; RT "Molecular epidemiology of methicillin-resistant staphylococci amongst RT veterinary personnel, personnel-owned pets, patients and the hospital RT environment of two companion animal veterinary hospitals."; RL Vet. Microbiol. 0:0-0(2018). CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides. CC {ECO:0000256|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:0000256|ARBA:ARBA00000870, CC ECO:0000256|HAMAP-Rule:MF_00550}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00550, CC ECO:0000256|PIRSR:PIRSR037215-2}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00550, CC ECO:0000256|PIRSR:PIRSR037215-2}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00550}. CC -!- SIMILARITY: Belongs to the peptidase M20B family. CC {ECO:0000256|ARBA:ARBA00009692, ECO:0000256|HAMAP-Rule:MF_00550}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PWZ99788.1}. 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; QEIV01000054; PWZ99788.1; -; Genomic_DNA. DR EMBL; QQPC01000062; REA80909.1; -; Genomic_DNA. DR RefSeq; WP_037543773.1; NZ_WWPQ01000053.1. DR AlphaFoldDB; A0A317ZD38; -. DR STRING; 937773.SPSINT_0455; -. DR OrthoDB; 9804934at2; -. DR Proteomes; UP000246351; Unassembled WGS sequence. DR Proteomes; UP000256409; Unassembled WGS sequence. 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. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP- KW Rule:MF_00550}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00550}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00550}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00550}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP- KW Rule:MF_00550}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00550}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|PIRSR:PIRSR037215-2}. FT DOMAIN 207..307 FT /note="Peptidase M20 dimerisation" FT /evidence="ECO:0000259|Pfam:PF07687" FT ACT_SITE 80 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550, FT ECO:0000256|PIRSR:PIRSR037215-1" FT ACT_SITE 174 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550, FT ECO:0000256|PIRSR:PIRSR037215-1" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550, FT ECO:0000256|PIRSR:PIRSR037215-2" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550, FT ECO:0000256|PIRSR:PIRSR037215-2" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550, FT ECO:0000256|PIRSR:PIRSR037215-2" FT BINDING 175 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550, FT ECO:0000256|PIRSR:PIRSR037215-2" FT BINDING 197 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550, FT ECO:0000256|PIRSR:PIRSR037215-2" FT BINDING 379 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550, FT ECO:0000256|PIRSR:PIRSR037215-2" SQ SEQUENCE 407 AA; 45430 MW; 74DED9A6B8D3EB90 CRC64; MKEQIIERLS RYVKINTQSD PNSETTPSTE RQWDLLHLLE SELKAMGLDT DLDRHGYLFA TLEANIETEA PTIGFLAHVD TSPDFNAANV NPQMIDNYDG GVITLGTSGR EINPEVFPDI LKVKGHTLMT TDGTSLLGAD DKAGVVEIME ALQYLIAHPE IKHGHIRVGF TPDEEIGRGP HKFDVERFDA DFAYTMDGSQ LGELQFESFN AAEAKITFNG VNVHPGSAKD KMVNALNLAN TFHQALPVNE VPEHTEGYEG FFHLMELNGN VEKATAQYII RDHDSTSFEN RKQQLIEIQK DINARYYYDP VHLVINDQYR NMAEKIKPLQ HIIDIPKAVY ADLNITPNTE PIRGGTDGSQ LSFMGLPTPN LFTGCDNFHG PYEYASIDVM AQAVQVILGI VQKVAEK //