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Database: UniProt
Entry: A0A415DUX1_9FIRM
LinkDB: A0A415DUX1_9FIRM
Original site: A0A415DUX1_9FIRM 
ID   A0A415DUX1_9FIRM        Unreviewed;       407 AA.
AC   A0A415DUX1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=tripeptide aminopeptidase {ECO:0000256|ARBA:ARBA00012563};
DE            EC=3.4.11.4 {ECO:0000256|ARBA:ARBA00012563};
GN   Name=pepT {ECO:0000313|EMBL:RHJ83736.1};
GN   ORFNames=DW099_18625 {ECO:0000313|EMBL:RHJ83736.1};
OS   Emergencia timonensis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis; Emergencia.
OX   NCBI_TaxID=1776384 {ECO:0000313|EMBL:RHJ83736.1, ECO:0000313|Proteomes:UP000284841};
RN   [1] {ECO:0000313|EMBL:RHJ83736.1, ECO:0000313|Proteomes:UP000284841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM07-24 {ECO:0000313|EMBL:RHJ83736.1,
RC   ECO:0000313|Proteomes:UP000284841};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR037215-2};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR037215-
CC       2};
CC   -!- SIMILARITY: Belongs to the peptidase M20B family.
CC       {ECO:0000256|ARBA:ARBA00009692}.
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:RHJ83736.1}.
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DR   EMBL; QRMS01000008; RHJ83736.1; -; Genomic_DNA.
DR   RefSeq; WP_067535162.1; NZ_QRMS01000008.1.
DR   AlphaFoldDB; A0A415DUX1; -.
DR   STRING; 1776384.GCA_900086585_01218; -.
DR   GeneID; 83003601; -.
DR   OrthoDB; 9804934at2; -.
DR   Proteomes; UP000284841; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 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.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:RHJ83736.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RHJ83736.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR037215-2};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284841};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT   DOMAIN          205..306
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        79
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         377
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
SQ   SEQUENCE   407 AA;  44928 MW;  B1F489C9D1F62BE3 CRC64;
     MRPYERFLNY VMFDTMSLEG QTTVPSTPGQ RTLAEALVSE LRGFGIEDVR LDDKGYIYGS
     VPSNIEKEVP VIGFIAHVDT SDAHPSPSKA PRIIENYDGS QIELAPGVLL DSANDSNLQN
     AIGCDIIVTD GTTLLGGDDK AGVAEIITAL EYMAEHQDFK HGKIAFSFTP DEEIGTSQDN
     FDVPAFGADF AYTVDGADFG DIEYENFYGA SLTVDIKGVS THPGEAKDKM KNASLIAMEF
     DALLPPWERP EHTQDYEGFY HLMHISGDCG HCQMNYIIRE HDYEKYQQRK TMALQGAEIL
     NQRYGEGTVS AEVKDGYRNM AEMVRPHMHL IDFAKEAIAQ CGVTPRVPAI RGGTDGSELS
     YKGVPCPNLG TGSFNHHSLT EVANIDHMDQ CTEVILKIIS RYAEFEA
//
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