PEPT_LACLM
ID PEPT_LACLM Reviewed; 413 AA.
AC A2RMN0; P42020; Q83U12; Q84BV4; Q84BV5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Peptidase T;
DE EC=3.4.11.4;
DE AltName: Full=Aminotripeptidase;
DE Short=Tripeptidase;
DE AltName: Full=Tripeptide aminopeptidase;
GN Name=pepT; OrderedLocusNames=llmg_1994;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8188586; DOI=10.1128/jb.176.10.2854-2861.1994;
RA Mierau I., Haandrikman A.J., Velterop O., Tan P.S.T., Leenhouts K.L.,
RA Konings W.N., Venema G., Kok J.;
RT "Tripeptidase gene (pepT) of Lactococcus lactis: molecular cloning and
RT nucleotide sequencing of pepT and construction of a chromosomal deletion
RT mutant.";
RL J. Bacteriol. 176:2854-2861(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides. Has a broad
CC specificity for tripeptides with no clear preference for a particular
CC tripeptide. Tripeptides with proline in the second position are an
CC exception and are not hydrolyzed. Does not hydrolyze dipeptides,
CC tetrapeptides, or oligopeptides (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of the N-terminal residue from a tripeptide.;
CC EC=3.4.11.4;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M20B family. {ECO:0000305}.
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DR EMBL; L27596; AAA20627.1; -; Genomic_DNA.
DR EMBL; AM406671; CAL98564.1; -; Genomic_DNA.
DR RefSeq; WP_011676821.1; NZ_WJVF01000004.1.
DR AlphaFoldDB; A2RMN0; -.
DR SMR; A2RMN0; -.
DR STRING; 416870.llmg_1994; -.
DR EnsemblBacteria; CAL98564; CAL98564; llmg_1994.
DR GeneID; 61110139; -.
DR KEGG; llm:llmg_1994; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_053676_0_0_9; -.
DR OMA; GHNFHGK; -.
DR PhylomeDB; A2RMN0; -.
DR BioCyc; LLAC416870:LLMG_RS09990-MON; -.
DR Proteomes; UP000000364; 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..413
FT /note="Peptidase T"
FT /id="PRO_0000285236"
FT ACT_SITE 83
FT /evidence="ECO:0000250"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 413 AA; 45946 MW; 6DFB82DFE8744E1F CRC64;
MKYEKLLPRF LEYVKVNTRS DENSTTTPST QALVEFAHKM GEDMKALGLK DVHYLESNGY
VIGTIPANTD KKVRKIGLLA HLDTADFNAE GVNPQILENY DGESVIQLGD TEFTLDPKDF
PNLKNYKGQT LVHTDGTTLL GSDDKSGVAE IMTLADYLLN INPDFEHGEI RVGFGPDEEI
GVGADKFDVA DFDVDFAYTV DGGPLGELQY ETFSAAGAVI EFQGKNVHPG TAKNMMVNAL
QLAIDYHNAL PEFDRPEKTE GREGFFHLLK LDGTPEEARA QYIIRDHEEG KFNERKALMQ
EIADKMNAEL GQNRVKPVIK DQYYNMAQII EKDMSIIDIA KKAMENLDIA PIIEPIRGGT
DGSKISFMGL PTPNLFAGGE NMHGRFEFVS VQTMEKAVDT LLEIIRLNNE VAK
