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Peptidase T (EC 3.4.11.4) (Aminotripeptidase) (Tripeptidase) (L9PepTR) (Tripeptide aminopeptidase)

 PEPT_LACLL              Reviewed;         413 AA.
Q76HM5;
07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 90.
RecName: Full=Peptidase T {ECO:0000255|HAMAP-Rule:MF_00550};
EC=3.4.11.4 {ECO:0000255|HAMAP-Rule:MF_00550, ECO:0000269|PubMed:15752689, ECO:0000269|PubMed:16233215};
AltName: Full=Aminotripeptidase {ECO:0000255|HAMAP-Rule:MF_00550, ECO:0000303|PubMed:16233215};
Short=Tripeptidase {ECO:0000255|HAMAP-Rule:MF_00550, ECO:0000303|PubMed:15752689, ECO:0000303|PubMed:16233215};
AltName: Full=L9PepTR {ECO:0000303|PubMed:15752689};
AltName: Full=Tripeptide aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
Name=pepT {ECO:0000255|HAMAP-Rule:MF_00550,
ECO:0000303|PubMed:15752689};
Lactococcus lactis subsp. lactis (Streptococcus lactis).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Lactococcus.
NCBI_TaxID=1360;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 13675 / LMG 9441 / NCDO 1007, NIAI N-7, NIRD DRC-1, and
NIRD DRC-2;
PubMed=15368846; DOI=10.1078/0723202041438400;
Mori S., Mori K., Suzuki I., Kasumi T.;
"Phylogenetic analysis of Lactococcus lactis subspecies based on
decoding the sequence of the pepT tripeptidase gene, the pepV
dipeptidase gene and 16S rRNA.";
Syst. Appl. Microbiol. 27:414-422(2004).
[2]
PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
STRAIN=ATCC 13675 / LMG 9441 / NCDO 1007;
PubMed=15752689; DOI=10.1016/j.bbapap.2004.12.001;
Mori S., Nirasawa S., Komba S., Kasumi T.;
"Characterization and kinetic analysis of enzyme-substrate recognition
by three recombinant lactococcal tripeptidases.";
Biochim. Biophys. Acta 1748:26-34(2005).
[3]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
SUBSTRATE SPECIFICITY, ENZYME REGULATION, AND SUBUNIT.
STRAIN=ATCC 13675 / LMG 9441 / NCDO 1007;
PubMed=16233215; DOI=10.1016/S1389-1723(02)80068-8;
Mori S., Sumino S., Kasumi T.;
"Substrate specificity of a tripeptidase as a metalloenzyme purified
from Lactococcus lactis subsp. lactis biovar. diacetylactis ATCC
13675.";
J. Biosci. Bioeng. 93:360-366(2002).
-!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides.
{ECO:0000255|HAMAP-Rule:MF_00550, ECO:0000269|PubMed:15752689,
ECO:0000269|PubMed:16233215}.
-!- CATALYTIC ACTIVITY: Release of the N-terminal residue from a
tripeptide. {ECO:0000255|HAMAP-Rule:MF_00550,
ECO:0000269|PubMed:15752689, ECO:0000269|PubMed:16233215}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_00550,
ECO:0000269|PubMed:16233215};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:16233215};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:16233215};
Note=Binds 2 Zn(2+) ions per subunit. To a lesser extent, can also
use Co(2+) or Mn(2+) instead of Zn(2+). {ECO:0000255|HAMAP-
Rule:MF_00550, ECO:0000269|PubMed:16233215};
-!- ENZYME REGULATION: Activity is strongly inhibited in vitro by
chelating agents such as EDTA and 1,10-phenanthroline as do the
reducing agent dithiothreitol and the oxidizing agent N-
bromosuccinimid. Phenylmethylsulfonyl fluoride, a serine protease
inhibitor has no influence on the enzyme activity. On the other
hand, bestatin, an aminopeptidase inhibitor strongly inhibits the
enzyme activity and leupeptin, a modified tripeptide, slightly
inhibits it. {ECO:0000269|PubMed:16233215}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.147 mM for AAA tripeptide {ECO:0000269|PubMed:15752689};
KM=0.390 mM for GAA tripeptide {ECO:0000269|PubMed:15752689};
KM=0.598 mM for AGA tripeptide {ECO:0000269|PubMed:15752689};
KM=1.29 mM for AAG tripeptide {ECO:0000269|PubMed:15752689};
KM=0.770 mM for GGA tripeptide {ECO:0000269|PubMed:15752689};
KM=1.57 mM for AGG tripeptide {ECO:0000269|PubMed:15752689};
KM=4.52 mM for GAG tripeptide {ECO:0000269|PubMed:15752689};
KM=12.0 mM for GGG tripeptide {ECO:0000269|PubMed:15752689};
KM=1.77 mM for YGG tripeptide {ECO:0000269|PubMed:15752689};
KM=2.44 mM for LGG tripeptide {ECO:0000269|PubMed:15752689};
KM=3.54 mM for FGG tripeptide {ECO:0000269|PubMed:15752689};
KM=6.49 mM for SGG tripeptide {ECO:0000269|PubMed:15752689};
KM=10.6 mM for AibGG tripeptide {ECO:0000269|PubMed:15752689};
Note=kcat is 163 sec(-1) with AAA tripeptide as substrate. kcat
is 616 sec(-1) with GAA tripeptide as substrate. kcat is 713
sec(-1) with AGA tripeptide as substrate. kcat is 730 sec(-1)
with AAG tripeptide as substrate. kcat is 507 sec(-1) with GGA
tripeptide as substrate. kcat is 573 sec(-1) with AGG tripeptide
as substrate. kcat is 1093 sec(-1) with GAG tripeptide as
substrate. kcat is 502 sec(-1) with GGG tripeptide as substrate.
kcat is 292 sec(-1) with YGG tripeptide as substrate. kcat is
197 sec(-1) with LGG tripeptide as substrate. kcat is 262 sec(-
1) with FGG tripeptide as substrate. kcat is 270 sec(-1) with
SGG tripeptide as substrate. kcat is 31.2 sec(-1) with AibGG
tripeptide as substrate. kcat is 453 sec(-1) with GGF tripeptide
as substrate. kcat is 806 sec(-1) with GAY tripeptide as
substrate. {ECO:0000269|PubMed:15752689};
pH dependence:
Optimum pH is around 8. The enzyme is stable in a pH range of 9-
10. {ECO:0000269|PubMed:15752689, ECO:0000269|PubMed:16233215};
Temperature dependence:
Optimum temperature is around 44 degrees Celsius. The enzyme is
stable up to 50 degrees Celsius. {ECO:0000269|PubMed:15752689,
ECO:0000269|PubMed:16233215};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15752689,
ECO:0000269|PubMed:16233215}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00550}.
-!- SIMILARITY: Belongs to the peptidase M20B family.
{ECO:0000255|HAMAP-Rule:MF_00550}.
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EMBL; AB100769; BAC66669.1; -; Genomic_DNA.
EMBL; AB100770; BAC66670.1; -; Genomic_DNA.
EMBL; AB100771; BAC66671.1; -; Genomic_DNA.
EMBL; AB100775; BAC66675.1; -; Genomic_DNA.
RefSeq; WP_003130321.1; NZ_MUBH01000003.1.
ProteinModelPortal; Q76HM5; -.
SMR; Q76HM5; -.
PaxDb; Q76HM5; -.
eggNOG; ENOG4105D42; Bacteria.
eggNOG; COG2195; LUCA.
SABIO-RK; Q76HM5; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0045148; F:tripeptide aminopeptidase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0006518; P:peptide metabolic process; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
CDD; cd03892; M20_peptT; 1.
HAMAP; MF_00550; Aminopeptidase_M20; 1.
InterPro; IPR001261; ArgE/DapE_CS.
InterPro; IPR036264; Bact_exopeptidase_dim_dom.
InterPro; IPR002933; Peptidase_M20.
InterPro; IPR011650; Peptidase_M20_dimer.
InterPro; IPR010161; Peptidase_M20B.
PANTHER; PTHR42994:SF1; PTHR42994:SF1; 1.
Pfam; PF07687; M20_dimer; 1.
Pfam; PF01546; Peptidase_M20; 1.
PIRSF; PIRSF037215; Peptidase_M20B; 1.
SUPFAM; SSF55031; SSF55031; 1.
TIGRFAMs; TIGR01882; peptidase-T; 1.
PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
1: Evidence at protein level;
Aminopeptidase; Cobalt; Cytoplasm; Direct protein sequencing;
Hydrolase; Manganese; Metal-binding; Metalloprotease; Protease; Zinc.
CHAIN 1 413 Peptidase T.
/FTId=PRO_0000431585.
ACT_SITE 83 83 {ECO:0000255|HAMAP-Rule:MF_00550}.
ACT_SITE 178 178 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00550}.
METAL 81 81 Zinc 1. {ECO:0000255|HAMAP-
Rule:MF_00550}.
METAL 143 143 Zinc 1. {ECO:0000255|HAMAP-
Rule:MF_00550}.
METAL 143 143 Zinc 2. {ECO:0000255|HAMAP-
Rule:MF_00550}.
METAL 179 179 Zinc 2. {ECO:0000255|HAMAP-
Rule:MF_00550}.
METAL 201 201 Zinc 1. {ECO:0000255|HAMAP-
Rule:MF_00550}.
METAL 383 383 Zinc 2. {ECO:0000255|HAMAP-
Rule:MF_00550}.
SEQUENCE 413 AA; 45972 MW; 52E26C8E7F518FEC CRC64;
MKYEKLLPRF LEYVKVNTRS DENSTTTPST QALVEFAHKM GEDMKALGLK DVHYLESNGY
VIGTIPANTD KKVRKIGLLA HLDTADFNAE GVNPQILENY DGESVIKLGD TEFTLDPKDF
PNLKNYKGQT LVHTDGTTLL GSDDKSGVAE IMTLADYLLN INPDFEHGEI RVGFGPDEEI
GVGADKFDVA DFDVDFAYTV DGGPLGELQY ETFSAAGAVI EFQGKNVHPG TAKNTMVNAL
QLAIDYHNAL PEFDRPEKTE GREGFFHLLK LDGTPEEARA QYIIRDHEEG KFNERKALMQ
EIADKMNAEL GQNRVKPVIK DQYYNMAQII EKDMSIIDIA KKAMENLDIV PIIEPIRGGT
DGSKISFMGL PTPNLFAGGE NMHGRFEFVS VQTMEKAVDT LLEIIRLNNE VVK


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