PEPT_STRP7
ID PEPT_STRP7 Reviewed; 407 AA.
AC C1C6Y4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=SP70585_1047;
OS Streptococcus pneumoniae (strain 70585).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70585;
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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; CP000918; ACO15860.1; -; Genomic_DNA.
DR RefSeq; WP_000222035.1; NC_012468.1.
DR AlphaFoldDB; C1C6Y4; -.
DR SMR; C1C6Y4; -.
DR MEROPS; M20.003; -.
DR EnsemblBacteria; ACO15860; ACO15860; SP70585_1047.
DR KEGG; snm:SP70585_1047; -.
DR HOGENOM; CLU_053676_0_0_9; -.
DR OMA; GHNFHGK; -.
DR Proteomes; UP000002211; 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..407
FT /note="Peptidase T"
FT /id="PRO_1000200899"
FT ACT_SITE 83
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 381
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; 44775 MW; 8A2E8AABCB970645 CRC64;
MTYPNLLDRF LTYVKVNTRS DEHSTTTPST QSQVDFATNV LIPEMKRVGL QNVYYLPNGF
AIGTLPANDP SLTRKIGFIS HMDTADFNAE GVNPQVIENY DGGVIELGNS GFKLDPADFK
SLEKYPGQTL ITTDGTSLLG ADDKSGIAEI MTAIEYLTAH PEIKHCEIRV GFGPDEEIGV
GANKFDAEDF DVDFAYTVDG GPLGELQYET FSAAGAELHF QGRNVHPGTA KGQMVNALQL
AIDFHNQLPE NDRPELTEGY QGFYHLMDVT GSVEEARASY IIRDFEKDAF EARKASMQSI
ADKMNEELGS DRVTLNLTDQ YYNMKEVIEK DMTPITIAKA VMEDLGITPI IEPIRGGTDG
SKISFMGIPT PNIFAGGENM HGRFEYVSLQ TMERAVDTII GIVAYKG
