PEPT_STRU0
ID PEPT_STRU0 Reviewed; 407 AA.
AC B9DU35;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=SUB0706;
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J;
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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; AM946015; CAR41615.1; -; Genomic_DNA.
DR RefSeq; WP_012658223.1; NC_012004.1.
DR AlphaFoldDB; B9DU35; -.
DR SMR; B9DU35; -.
DR STRING; 218495.SUB0706; -.
DR MEROPS; M20.003; -.
DR EnsemblBacteria; CAR41615; CAR41615; SUB0706.
DR KEGG; sub:SUB0706; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_053676_0_0_9; -.
DR OMA; GHNFHGK; -.
DR OrthoDB; 1015417at2; -.
DR Proteomes; UP000000449; 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; Reference proteome; Zinc.
FT CHAIN 1..407
FT /note="Peptidase T"
FT /id="PRO_1000200904"
FT ACT_SITE 84
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
SQ SEQUENCE 407 AA; 45137 MW; 0614A14AE7A481C4 CRC64;
MVYNNLLERF IKYVKVNTRS NPTSQTTPST QSQVDFALQV LKPEMEAIGL EDVHYLEHNG
YIVGTLPANA QHLTRKIGFI SHMDTADFNA EGINPQVIDN YEGGNITLGQ SGYLLKPDDF
PQLNNYLGQT LVTTDGTTLL GADDKSGIAE IMTAIEFLVA NPTIEHCEIR VAFGPDEEIG
TGANKFDVED FNVDFAYTVD GGPLGELQYE TFSAAGLDVQ FLGRNVHPGT AKGQMINALQ
LAIDFHNQLP ETDRPEKTDG YQGFYHLLDL SGTVEEASSS YIIRDFEDDS FKSRKAFIEQ
LAQKMNDELG ENRVVISLQD QYYNMKKVIE KDMTPVNLAK EVMEDLDIKP IIEPIRGGTD
GSKISFMGIP TPNIFAGGEN MHGRFEFVSL ETMEKAVDVI LGIVQKP