PEPT_LACLC
ID PEPT_LACLC Reviewed; 413 AA.
AC P0C2T7; P42020; Q83U12; Q84BV4; Q84BV5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
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;
OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19257 / DSM 20069 / BCRC 12586 / JCM 16167 / LMG 6897 / NBRC
RC 100676 / NCDO 607 / NCIMB 8662 / HP, NIAI H-61, NIRD HC-1, and NIRD Ho-6;
RX PubMed=15368846; DOI=10.1078/0723202041438400;
RA Mori S., Mori K., Suzuki I., Kasumi T.;
RT "Phylogenetic analysis of Lactococcus lactis subspecies based on decoding
RT the sequence of the pepT tripeptidase gene, the pepV dipeptidase gene and
RT 16S rRNA.";
RL Syst. Appl. Microbiol. 27:414-422(2004).
RN [2]
RP PROTEIN SEQUENCE OF 1-20.
RC STRAIN=Wg2;
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 [3]
RP FUNCTION, CHARACTERIZATION, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT,
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Wg2;
RX PubMed=16348224; DOI=10.1128/aem.56.6.1839-1843.1990;
RA Bosman B.W., Tan P.S.T., Konings W.N.;
RT "Purification and characterization of a tripeptidase from Lactococcus
RT lactis subsp. cremoris Wg2.";
RL Appl. Environ. Microbiol. 56:1839-1843(1990).
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. {ECO:0000269|PubMed:16348224}.
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;
CC Evidence={ECO:0000305|PubMed:16348224};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000305|PubMed:16348224};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, by the reducing agents
CC dithiothreitol and 13-mercaptoethanol, and by the divalent cation
CC Cu(2+). {ECO:0000269|PubMed:16348224}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.15 mM for tripeptide Leu-Leu-Leu {ECO:0000269|PubMed:16348224};
CC Vmax=151 umol/min/mg enzyme with Leu-Leu-Leu as substrate
CC {ECO:0000269|PubMed:16348224};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:16348224};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:16348224};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16348224}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M20B family. {ECO:0000305}.
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; AB100761; BAC66661.1; -; Genomic_DNA.
DR EMBL; AB100762; BAC66662.1; -; Genomic_DNA.
DR EMBL; AB100763; BAC66663.1; -; Genomic_DNA.
DR EMBL; AB100772; BAC66672.1; -; Genomic_DNA.
DR RefSeq; WP_032950431.1; NZ_VERZ01000075.1.
DR AlphaFoldDB; P0C2T7; -.
DR SMR; P0C2T7; -.
DR SABIO-RK; P0C2T7; -.
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 1: Evidence at protein level;
KW Aminopeptidase; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Zinc.
FT CHAIN 1..413
FT /note="Peptidase T"
FT /id="PRO_0000185301"
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"
FT VARIANT 48
FT /note="G -> R (in strain: ATCC 19257)"
FT VARIANT 94
FT /note="P -> S (in strain: ATCC 19257)"
FT VARIANT 191
FT /note="D -> E (in strain: NIRD HC-1)"
FT VARIANT 318
FT /note="L -> V (in strain: ATCC 19257 and NIRD HC-1)"
SQ SEQUENCE 413 AA; 45960 MW; 960F3D941CDFAE04 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 GQNRVKPLIK DQYYNMAQII EKDMSIIDIA KKAMENLDIA PIIEPIRGGT
DGSKISFMGL PTPNLFAGGE NMHGRFEFVS VQTMEKAVDT LLEIIRLNNE VAK
