ID F3YAA6_MELPT Unreviewed; 413 AA.
AC F3YAA6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Peptidase T {ECO:0000256|HAMAP-Rule:MF_00550};
DE EC=3.4.11.4 {ECO:0000256|HAMAP-Rule:MF_00550};
DE AltName: Full=Aminotripeptidase {ECO:0000256|HAMAP-Rule:MF_00550};
DE Short=Tripeptidase {ECO:0000256|HAMAP-Rule:MF_00550};
DE AltName: Full=Tripeptide aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00550};
GN Name=pepT {ECO:0000256|HAMAP-Rule:MF_00550};
GN OrderedLocusNames=MPTP_0975 {ECO:0000313|EMBL:BAK21434.1};
OS Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB
OS 702443).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Melissococcus.
OX NCBI_TaxID=940190 {ECO:0000313|EMBL:BAK21434.1, ECO:0000313|Proteomes:UP000008456};
RN [1] {ECO:0000313|EMBL:BAK21434.1, ECO:0000313|Proteomes:UP000008456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443
RC {ECO:0000313|Proteomes:UP000008456};
RX PubMed=21622755; DOI=10.1128/JB.05151-11;
RA Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M.,
RA Miyoshi-Akiyama T.;
RT "Complete genome sequence of Melissococcus plutonius ATCC 35311.";
RL J. Bacteriol. 193:4029-4030(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 35311;
RA Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D.,
RA Akiyama T.;
RT "Whole genome sequence of Melissococcus plutonius ATCC 35311.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides.
CC {ECO:0000256|HAMAP-Rule:MF_00550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of the N-terminal residue from a tripeptide.;
CC EC=3.4.11.4; Evidence={ECO:0000256|ARBA:ARBA00000870,
CC ECO:0000256|HAMAP-Rule:MF_00550};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00550,
CC ECO:0000256|PIRSR:PIRSR037215-2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00550,
CC ECO:0000256|PIRSR:PIRSR037215-2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00550}.
CC -!- SIMILARITY: Belongs to the peptidase M20B family.
CC {ECO:0000256|ARBA:ARBA00009692, ECO:0000256|HAMAP-Rule:MF_00550}.
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; AP012200; BAK21434.1; -; Genomic_DNA.
DR RefSeq; WP_013773872.1; NC_015516.1.
DR AlphaFoldDB; F3YAA6; -.
DR STRING; 940190.MPTP_0975; -.
DR MEROPS; M20.003; -.
DR KEGG; mps:MPTP_0975; -.
DR HOGENOM; CLU_053676_0_0_9; -.
DR OrthoDB; 9804934at2; -.
DR Proteomes; UP000008456; 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 CDD; cd03892; M20_peptT; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
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 NCBIfam; TIGR01882; peptidase-T; 1.
DR PANTHER; PTHR42994; PEPTIDASE T; 1.
DR PANTHER; PTHR42994:SF1; PEPTIDASE T; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037215; Peptidase_M20B; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW Rule:MF_00550}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00550};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00550};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00550};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_00550};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00550};
KW Reference proteome {ECO:0000313|Proteomes:UP000008456};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 210..310
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 83
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-1"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-1"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-2"
SQ SEQUENCE 413 AA; 46199 MW; 92FF814D4644BEBB CRC64;
MYENLLPRFL RYVKIETRSN EQSETTPSTQ SQVDFAQLLK IELEELGLDD VIYNEANGYV
IATLPGNCPD KEVRTLGFIA HMDTADFNAE QVKPQIIENY DGESTINLDK KGKYTLNTSD
FPNLRNYTGE TLITTDGTTL LGSDDKSGIA EIMTAMEFLL NHPQIKHGTI RIAFGPDEEI
GRGADKFDVK QFNVDFAYTV DGGPLGELQY ETFNAAQAEI TIEGKNVHPG TAKNTMINAL
QLAVDFHNQL PANEVPEKTE GYEGFYHLAS LEGTPDSAKM TYIIRDHHAE KFNDRKKMIT
TIQKNMNSKL DAERIHVHLF DQYYNMRSII EKDLSIVELA KKAMLALNIK PIIEPVRGGT
DGSKISFLGT PTPNIFAGGE NMHGRYEFVS LQSMEKATGV IIKIAELNSK SEQ
//
