ID A0A317ZD38_STAPS Unreviewed; 407 AA. AC A0A317ZD38; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 07-NOV-2018, entry version 2. 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=DD881_05745 {ECO:0000313|EMBL:PWZ85307.1}, DD924_00790 GN {ECO:0000313|EMBL:PWZ99788.1}; OS Staphylococcus pseudintermedius. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=283734 {ECO:0000313|EMBL:PWZ99788.1, ECO:0000313|Proteomes:UP000246351}; RN [1] {ECO:0000313|EMBL:PWZ99788.1, ECO:0000313|Proteomes:UP000246351, ECO:0000313|Proteomes:UP000246542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST496 1 {ECO:0000313|EMBL:PWZ85307.1, RC ECO:0000313|Proteomes:UP000246542}, and ST71 3 RC {ECO:0000313|EMBL:PWZ99788.1, ECO:0000313|Proteomes:UP000246351}; RX PubMed=29292005; RA Worthing K.A., Abraham S., Coombs G.W., Pang S., Saputra S., RA Jordan D., Trott D.J., Norris J.M.; RT "Clonal diversity and geographic distribution of methicillin-resistant RT Staphylococcus pseudintermedius from Australian animals: Discovery of RT novel sequence types."; RL Vet. Microbiol. 213:58-65(2018). CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides. CC {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|SAAS:SAAS00756406}. CC -!- CATALYTIC ACTIVITY: Release of the N-terminal residue from a CC tripeptide. {ECO:0000256|HAMAP-Rule:MF_00550, CC ECO:0000256|SAAS:SAAS00756399}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00550}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00550}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00550, CC ECO:0000256|SAAS:SAAS00756389}. CC -!- SIMILARITY: Belongs to the peptidase M20B family. CC {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|SAAS:SAAS00756409}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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; QEJK01000022; PWZ85307.1; -; Genomic_DNA. DR EMBL; QEIV01000054; PWZ99788.1; -; Genomic_DNA. DR RefSeq; WP_037543773.1; NZ_QQPJ01000001.1. DR Proteomes; UP000246351; Unassembled WGS sequence. DR Proteomes; UP000246542; Unassembled WGS sequence. DR CDD; cd03892; M20_peptT; 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 PANTHER; PTHR42994:SF1; PTHR42994:SF1; 1. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF037215; Peptidase_M20B; 1. DR SUPFAM; SSF55031; SSF55031; 1. DR TIGRFAMs; TIGR01882; peptidase-T; 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|HAMAP-Rule:MF_00550, KW ECO:0000256|SAAS:SAAS00756408}; KW Complete proteome {ECO:0000313|Proteomes:UP000246351, KW ECO:0000313|Proteomes:UP000246542}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00550, KW ECO:0000256|SAAS:SAAS00756401}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00550, KW ECO:0000256|SAAS:SAAS00786827}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00550, KW ECO:0000256|SAAS:SAAS00786925}; KW Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00550, KW ECO:0000256|SAAS:SAAS00756410}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00550, KW ECO:0000256|SAAS:SAAS00756386}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|SAAS:SAAS00756404}. FT DOMAIN 208 306 M20_dimer. {ECO:0000259|Pfam:PF07687}. FT ACT_SITE 80 80 {ECO:0000256|HAMAP-Rule:MF_00550}. FT ACT_SITE 174 174 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00550}. FT METAL 78 78 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_00550}. FT METAL 140 140 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_00550}. FT METAL 140 140 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00550}. FT METAL 175 175 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00550}. FT METAL 197 197 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_00550}. FT METAL 379 379 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00550}. 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 //