ID A0A0A2FBC9_9PORP Unreviewed; 415 AA.
AC A0A0A2FBC9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ORFNames=HQ41_02765 {ECO:0000313|EMBL:KGN85734.1};
OS Porphyromonas sp. COT-290 OH860.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1515615 {ECO:0000313|EMBL:KGN85734.1, ECO:0000313|Proteomes:UP000030116};
RN [1] {ECO:0000313|EMBL:KGN85734.1, ECO:0000313|Proteomes:UP000030116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-290 OH860 {ECO:0000313|Proteomes:UP000030116};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas sp. strain:COT-290_OH860 Genome sequencing.";
RL Submitted (AUG-2014) 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|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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGN85734.1}.
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DR EMBL; JRAR01000020; KGN85734.1; -; Genomic_DNA.
DR RefSeq; WP_044187534.1; NZ_JRAR01000020.1.
DR AlphaFoldDB; A0A0A2FBC9; -.
DR MEROPS; M20.003; -.
DR eggNOG; COG2195; Bacteria.
DR OrthoDB; 9804934at2; -.
DR Proteomes; UP000030116; Unassembled WGS sequence.
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|HAMAP-Rule:MF_00550,
KW ECO:0000313|EMBL:KGN85734.1}; 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:UP000030116};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 215..311
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 89
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-1"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-1"
FT BINDING 87
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 149
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 149
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 184
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 206
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 388
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 415 AA; 46421 MW; 04EA91233E11E3F0 CRC64;
MKQIAQEVRE ELLERFLRYV AIDTQSDERS ETFPSTEKQL TLLNMLKDEL LVLGVSNARL
DQYGYVMASL PATPGYEEAT QIGFIAHVDT SPDLSGADVR PQLINNYQGE DIRLGTSDYV
LSPKQFPDLE LHLGHDLITT DGTTLLGADD KAGVAEIMTF VAYLMRHPEV AHGPISIGFT
PDEEIGRGVD HFDVKRFGAQ YAYTVDGSQE GELEYENFNA ASARIDVQGR NVHPGYAKGK
MINALQVLHD IHSLLPEAMR PECTSGYEGF YHLIGMSGSV DQAHASYIIR DHDRALFEEK
KAALERAVQT VNTKIGTRVA TLELRDQYYN MREQVLPHWA LIERAERAME RAGVRPLIRP
IRGGTDGSRL SYMGLPCPNL FAGGMNFHGR YEYASLTTMC RAVATLVHLA NLWRE
//
