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Database: UniProt
Entry: A0A1Y4TLE0_9FIRM
LinkDB: A0A1Y4TLE0_9FIRM
Original site: A0A1Y4TLE0_9FIRM 
ID   A0A1Y4TLE0_9FIRM        Unreviewed;       405 AA.
AC   A0A1Y4TLE0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=tripeptide aminopeptidase {ECO:0000256|ARBA:ARBA00012563};
DE            EC=3.4.11.4 {ECO:0000256|ARBA:ARBA00012563};
GN   ORFNames=B5E65_05755 {ECO:0000313|EMBL:OUQ43275.1};
OS   Gemmiger sp. An120.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Gemmiger.
OX   NCBI_TaxID=1965549 {ECO:0000313|EMBL:OUQ43275.1, ECO:0000313|Proteomes:UP000195783};
RN   [1] {ECO:0000313|Proteomes:UP000195783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An120 {ECO:0000313|Proteomes:UP000195783};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUQ43275.1}.
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DR   EMBL; NFLN01000004; OUQ43275.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4TLE0; -.
DR   OrthoDB; 9804934at2; -.
DR   Proteomes; UP000195783; 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   CDD; cd03892; M20_peptT; 1.
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.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037215-2};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195783};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT   DOMAIN          207..307
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT   ACT_SITE        173
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="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|PIRSR:PIRSR037215-2"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
SQ   SEQUENCE   405 AA;  44175 MW;  3B84C322AECEFFB4 CRC64;
     MRAYERFLDY VKVHTTSDDT TGTHPSTPGQ FDLARLLADQ MRALGLENVR VNETCYVYGF
     LPATPGCEDK PAIGLIAHMD TSPAASGEGV KPQLIENYDG NDVRLPATGD VMEVSRFPAL
     AACKGETLIT ADGSTLLGAD DKAGIAEILT AVERLQAENR PHGRICVAFT PDEEIGEGAD
     NFDVAGFGAD FAYTVDGGDV GELEYCNFNA ASAVFTVHGF SVHPGSAKGL MKNASNLAME
     LHAMLPASER PETTEGTEGF YHLDRLTGSV SEAKLEYIVR DHDREKFEAR KAFLRQVAET
     MNNTYGPGTV ELELRDSYYN MEEKIRPHFH LIENARIAIE QAGLEAKELP IRGGTDGARL
     SWMGLPCPNL GTGGFNFHGP CEFITAERMD KSVEILLNIL SLYIR
//
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