ID A0A2P8GK00_9BACL Unreviewed; 407 AA.
AC A0A2P8GK00;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=B0H99_10915 {ECO:0000313|EMBL:PSL34289.1};
OS Planomicrobium soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planomicrobium.
OX NCBI_TaxID=1176648 {ECO:0000313|EMBL:PSL34289.1, ECO:0000313|Proteomes:UP000242682};
RN [1] {ECO:0000313|EMBL:PSL34289.1, ECO:0000313|Proteomes:UP000242682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12259 {ECO:0000313|EMBL:PSL34289.1,
RC ECO:0000313|Proteomes:UP000242682};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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 -!- 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:PSL34289.1}.
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DR EMBL; PYAT01000009; PSL34289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8GK00; -.
DR OrthoDB; 9804934at2; -.
DR Proteomes; UP000242682; 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|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 Zinc {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 206..306
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 81
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-1"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-1"
FT BINDING 79
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 140
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 140
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 175
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 197
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 379
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 407 AA; 45198 MW; 4EFE708D42C47DB9 CRC64;
MLETLIERLV RYAKIDTQSD FTSTSTPSTP GQWDLLHELE REMKAIGLEE VGMDEHGYLF
GTLPSNTDKE LPVIGFLAHV DTATDFTGKN VNPQRVENYD GNDIALSDTV IMSPDDFPAL
KNYVGHTLIT TDGTTLLGAD NKAGIAEIMT AMEYLVQHPE ITHGKIRVAF TPDEEIGKGP
HKFDVAKFGA DFAYTMDGGP LGELQYESFN AAAAKLTVQG KSVHPGSSKN KMVNASTVAI
RFQQEMPKSE VPELTEDYEG FIHLNSFHGD VEKAELSYII RYFDKDEFEA KKAYMQQVAE
KLQSEYGAGA INLEIEDQYY NMREKIEPVM EIVDSAETAL KTLGIEPNIV PVRGGTDGSQ
LSYMGMPTPN IFTGGENYHG KYEFISAENM EKATQVIVEI VRSMEQK
//
