ID R6W2H1_9BACT Unreviewed; 407 AA.
AC R6W2H1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=BN725_01670 {ECO:0000313|EMBL:CDD05248.1};
OS Prevotella sp. CAG:592.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262931 {ECO:0000313|EMBL:CDD05248.1, ECO:0000313|Proteomes:UP000018343};
RN [1] {ECO:0000313|EMBL:CDD05248.1, ECO:0000313|Proteomes:UP000018343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:592 {ECO:0000313|Proteomes:UP000018343};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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|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:CDD05248.1}.
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DR EMBL; CBGI010000131; CDD05248.1; -; Genomic_DNA.
DR AlphaFoldDB; R6W2H1; -.
DR MEROPS; M20.003; -.
DR Proteomes; UP000018343; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000018343};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 204..307
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; 45249 MW; 9915DBF26C9DDDF3 CRC64;
MNITERFLNY VKFDTQSAEE SQTVPSTSKQ LIFAEYLRDE LKAEGFADVE MDEQGYIYAT
LKANTKKEIP TIGFISHYDT SPDCSGKDVK PRIVKAYDGG DIVLSEGIVS SPKKFPELLA
HKGEDLIVTD GHTLLGADDK AGIAEIVQAM CWLRDHDEIK HGDIRMGFNP DEEIGMGAHH
FNVEKFGCQW AYTIDGGDLG DLEYENFNAA AAKININGVS VHPGFAKGKM VNASMLATEL
AGMMPADERP ETTEGYEGFY HLLGIESNTE HAKMSYIIRD HDRKKFEDRK KFIVSVVDKM
NEKYGEGTVE IAVNDQYYNM KEKIDPNMHV IDIVLKAMEL CGVPPKVQPI RGGTDGAQLS
FKGLPCPNIF TGGVNFHGPY EFVSIQVMEK AMQTVVKICE LTAGYND
//
