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Database: UniProt
Entry: D8DUS1_PREBR
LinkDB: D8DUS1_PREBR
Original site: D8DUS1_PREBR 
ID   D8DUS1_PREBR            Unreviewed;       407 AA.
AC   D8DUS1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
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   ECO:0000313|EMBL:EFI72761.1};
GN   ORFNames=PBR_1822 {ECO:0000313|EMBL:EFI72761.1};
OS   Prevotella bryantii B14.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=752555 {ECO:0000313|EMBL:EFI72761.1, ECO:0000313|Proteomes:UP000004524};
RN   [1] {ECO:0000313|EMBL:EFI72761.1, ECO:0000313|Proteomes:UP000004524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B14 {ECO:0000313|EMBL:EFI72761.1,
RC   ECO:0000313|Proteomes:UP000004524};
RX   PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG   North American Consortium for Rumen Bacteria;
RA   Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA   Coutinho P.M., Henrissat B., Nelson K.E.;
RT   "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT   bryantii: insights into their environmental niche.";
RL   Microb. Ecol. 60:721-729(2010).
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:EFI72761.1}.
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DR   EMBL; ADWO01000026; EFI72761.1; -; Genomic_DNA.
DR   RefSeq; WP_006281769.1; NZ_FOEM01000001.1.
DR   STRING; 77095.SAMN05216455_101520; -.
DR   MEROPS; M20.003; -.
DR   GeneID; 72480440; -.
DR   OrthoDB; 9804934at2; -.
DR   Proteomes; UP000004524; 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:EFI72761.1}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00550};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00550};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00550,
KW   ECO:0000256|PIRSR:PIRSR037215-2};
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:UP000004524};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|PIRSR:PIRSR037215-2}.
FT   DOMAIN          204..306
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        79
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT                   ECO:0000256|PIRSR:PIRSR037215-1"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT                   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|HAMAP-Rule:MF_00550,
FT                   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|HAMAP-Rule:MF_00550,
FT                   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|HAMAP-Rule:MF_00550,
FT                   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|HAMAP-Rule:MF_00550,
FT                   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|HAMAP-Rule:MF_00550,
FT                   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|HAMAP-Rule:MF_00550,
FT                   ECO:0000256|PIRSR:PIRSR037215-2"
SQ   SEQUENCE   407 AA;  45683 MW;  593406D7808B9EE2 CRC64;
     MEITERFINY TKFDTQSSED SDCVPSTAKQ LEFAKYLKKE LEDEKFSDVE MDEMGYIYAT
     LKANTKKNIP TIGFISHYDT SPDCSGKDIK ARIVKNYDGN DIELSPGIIS STAKFPELKE
     HIGEDLIVTD GTTLLGADDK AGIAEIMQAM CYLRDHDEIK HGDIRVGFNP DEEIGMGAHH
     FDVEKFGCEW AYTMDGGDLG DLEYENFNAA SAKIHIKGVS VHPGYAKDKM INANRLAVEF
     QNMIPADQTP ECTEGYEGFY HLLHLEGSIE EAQLSYIIRD HDRDKFEDRK KYIANCAEKL
     NEKYGQGTCT VELHDQYYNM KEKIEPNMHV IDIVLKAMQE TGVPPRVAPI RGGTDGAQLS
     FKGLPCPNIF AGGVNYHGPY EFVSVQVMEK AVQTIVKICE ITAAFND
//
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