PEPT_LACLH
ID PEPT_LACLH Reviewed; 413 AA.
AC Q84BV2;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Tripeptide aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
DE AltName: Full=hTPepTR {ECO:0000303|PubMed:15752689};
GN Name=pepT {ECO:0000255|HAMAP-Rule:MF_00550, ECO:0000303|PubMed:15752689};
OS Lactococcus lactis subsp. hordniae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=203404;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29071 / DSM 20450 / JCM 1180 / KCTC 3768 / NBRC 100931 / NCDO
RC 2181 / NCIMB 702181 / HC-1;
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=ATCC 29071 / DSM 20450 / JCM 1180 / KCTC 3768 / NBRC 100931 / NCDO
RC 2181 / NCIMB 702181 / HC-1;
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 639 sec(-1) with GGF tripeptide as substrate. kcat is
CC 915 sec(-1) with GGA tripeptide as substrate. kcat is 1015 sec(-1)
CC with GAA tripeptide as substrate. kcat is 1219 sec(-1) with GAY
CC tripeptide as substrate. kcat is 373 sec(-1) with AAA tripeptide as
CC substrate. kcat is 1640 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 slightly lower than 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; AB100774; BAC66674.1; -; Genomic_DNA.
DR RefSeq; WP_058210196.1; NZ_VXKC01000010.1.
DR AlphaFoldDB; Q84BV2; -.
DR SMR; Q84BV2; -.
DR SABIO-RK; Q84BV2; -.
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_0000431584"
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; 45993 MW; 0E9BEF689DA471D9 CRC64;
MKYEKLLPRF LEYVKVNTRS DENSTTTPST QALVEFAHKM GEDMKALGLK DVHYLESNGY
VIGTIPANTD KKVRKIGLLA HLDTADFNAE GVNPQILENY DGESVIKLGD TEFTLDPKDF
PSLKNYKGQT LVHTDGTTLL GSDDKSGVAE IMTLAEYLLN INPDFEHGEI RVGFGPDEEI
GVGADKFDVA DFDVDFAYTV DGGPLGELQY ETFSAAGAVI EFQGKNVHPG TAKNTMVNAL
QLAIDYHNAL PEFDRPEKTE GREGFFHLLK LDGTPEEARA QYIIRDHEEG KFNERKALMQ
EIADKMNAEF GQNRVKPVIK DQYYNMAQII EKDMSIIDIA KKAMENLDIV PIIEPIRGGT
DGSKISFMGL PTPNLFAGGE NMHGRFEFVS VQTMEKAVDT LLEIIRLNNE VVK
