ID   PEPT_STAHJ              Reviewed;         409 AA.
AC   Q4L4G8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 126.
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}; OrderedLocusNames=SH2148;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; AP006716; BAE05457.1; -; Genomic_DNA.
DR   RefSeq; WP_011276410.1; NC_007168.1.
DR   AlphaFoldDB; Q4L4G8; -.
DR   SMR; Q4L4G8; -.
DR   STRING; 279808.SH2148; -.
DR   MEROPS; M20.003; -.
DR   EnsemblBacteria; BAE05457; BAE05457; SH2148.
DR   KEGG; sha:SH2148; -.
DR   eggNOG; COG2195; Bacteria.
DR   HOGENOM; CLU_053676_0_0_9; -.
DR   OMA; GHNFHGK; -.
DR   OrthoDB; 1015417at2; -.
DR   Proteomes; UP000000543; 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   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; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Zinc.
FT   CHAIN           1..409
FT                   /note="Peptidase T"
FT                   /id="PRO_1000129049"
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   409 AA;  46082 MW;  7BA0DBA88019F3C3 CRC64;
     MKAQLIDRLS RYVKIDTQSN PESSTTPSTE KQWDLLRLLQ QELEGFGLET NLDDNGYLFA
     TLESNVSFDV PTVGFLAHVD TSPDFNASNV NPQIVEQYDG KTIKLGDTGR VLSQETFPEL
     KKLIGHTLMI TDGTSLLGAD DKAGVVEIME AVKYLIEHPE IKHGRIRIAF TPDEEIGRGP
     HKFDVERFNA DFAYTMDGSE FGELQFESFN AAEANITTHG VNVHPGSAKN IMVNAISLGH
     QFHSLLPAGE VPERTEDYEG FYHLMKFEGN VEKATLQYII RDHDRESFEL RKKKLLEIRD
     DINVHYEDFP VKVDIEDQYY NMAEKIEPHP YIIDIPKKVF NDLNIEPNTA PIRGGTDGSQ
     LSFKGLPTPN IFTGCGNFHG PFEYASIDVM EKAVQVIIGI AQEVTHHHK