PEPT2_LACLC
ID PEPT2_LACLC Reviewed; 413 AA.
AC Q76HM7;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Peptidase T {ECO:0000255|HAMAP-Rule:MF_00550};
DE EC=3.4.11.4 {ECO:0000255|HAMAP-Rule:MF_00550, ECO:0000269|PubMed:15752689};
DE AltName: Full=Aminotripeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
DE Short=Tripeptidase {ECO:0000255|HAMAP-Rule:MF_00550, ECO:0000303|PubMed:15752689};
DE AltName: Full=L6PepTR {ECO:0000303|PubMed:15752689};
DE AltName: Full=Tripeptide aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
GN Name=pepT {ECO:0000255|HAMAP-Rule:MF_00550, ECO:0000303|PubMed:15752689};
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=NIAI SLN, and NIRD 712;
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 N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NIRD 712;
RX PubMed=15752689; DOI=10.1016/j.bbapap.2004.12.001;
RA Mori S., Nirasawa S., Komba S., Kasumi T.;
RT "Characterization and kinetic analysis of enzyme-substrate recognition by
RT three recombinant lactococcal tripeptidases.";
RL Biochim. Biophys. Acta 1748:26-34(2005).
CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides.
CC {ECO:0000255|HAMAP-Rule:MF_00550, ECO:0000269|PubMed:15752689}.
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 ECO:0000269|PubMed:15752689};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 355 sec(-1) with GGF tripeptide as substrate. kcat is
CC 437 sec(-1) with GGA tripeptide as substrate. kcat is 850 sec(-1)
CC with GAA tripeptide as substrate. kcat is 1050 sec(-1) with GAY
CC tripeptide as substrate. kcat is 240 sec(-1) with AAA tripeptide as
CC substrate. kcat is 1230 sec(-1) with AAG tripeptide as substrate.
CC {ECO:0000269|PubMed:15752689};
CC pH dependence:
CC Optimum pH is around 8. {ECO:0000269|PubMed:15752689};
CC Temperature dependence:
CC Optimum temperature is around 40 degrees Celsius.
CC {ECO:0000269|PubMed:15752689};
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; AB100766; BAC66666.1; -; Genomic_DNA.
DR EMBL; AB100767; BAC66667.1; -; Genomic_DNA.
DR RefSeq; WP_011676821.1; NZ_WJUX01000066.1.
DR AlphaFoldDB; Q76HM7; -.
DR SMR; Q76HM7; -.
DR GeneID; 61110139; -.
DR OMA; GHNFHGK; -.
DR SABIO-RK; Q76HM7; -.
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; IDA:UniProtKB.
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:0006518; P:peptide metabolic process; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
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_0000431586"
FT ACT_SITE 83
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT ACT_SITE 178
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 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 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
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
