PEPT_BACFN
ID PEPT_BACFN Reviewed; 407 AA.
AC Q5LFT7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Peptidase T {ECO:0000255|HAMAP-Rule:MF_00550};
DE EC=3.4.11.4 {ECO:0000255|HAMAP-Rule:MF_00550};
DE AltName: Full=Aminotripeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
DE Short=Tripeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
DE AltName: Full=Tripeptide aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
GN Name=pepT {ECO:0000255|HAMAP-Rule:MF_00550}; OrderedLocusNames=BF1289;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00550};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00550};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00550};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00550}.
CC -!- SIMILARITY: Belongs to the peptidase M20B family. {ECO:0000255|HAMAP-
CC 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; CR626927; CAH07006.1; -; Genomic_DNA.
DR RefSeq; WP_005786005.1; NC_003228.3.
DR AlphaFoldDB; Q5LFT7; -.
DR SMR; Q5LFT7; -.
DR STRING; 272559.BF9343_1225; -.
DR MEROPS; M20.003; -.
DR EnsemblBacteria; CAH07006; CAH07006; BF9343_1225.
DR GeneID; 66329793; -.
DR KEGG; bfs:BF9343_1225; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_053676_0_0_10; -.
DR OMA; GHNFHGK; -.
DR OrthoDB; 1015417at2; -.
DR Proteomes; UP000006731; 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 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 PANTHER; PTHR42994:SF1; PTHR42994:SF1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037215; Peptidase_M20B; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01882; peptidase-T; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..407
FT /note="Peptidase T"
FT /id="PRO_0000185286"
FT ACT_SITE 79
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
SQ SEQUENCE 407 AA; 45485 MW; 5BD553EA73E966C7 CRC64;
MNLVERFLKY VSFDTQSDEL TRLTPSTPGQ MVFAEYLKSE LESLGLEDIT LDENGYLFAT
LPANTEKELP VIGFIAHMDT SPDMSGKNVT PRIVEKYDGS DIVLCAEENI VLSPSQFPEL
LDHKGEDLIV TNGKTLLGAD DKAGIAEIVS AVVYLQEHPE IKHGKIRIGF NPDEEIGEGA
HKFDVQKFGC EWAYTMDGGE VGELEFENFN AAAAKITFKG RNVHPGYAKH KMINSIRIAN
QFITMLPRHE TPEHTSGYEG FYHLIGIQGD VEQSTVSYII RDHDRNKFED RKKEIEHLVN
KINAEFGEGT ATLELRDQYY NMREKIEPVM HIIDTAFAAM EAVGVKPNVK PIRGGTDGAQ
LSFKGLPCPN IFAGGLNFHG RYEFVPIQNM EKAMKVIVKI AELVASK
