ID U3U2F0_9ENTR Unreviewed; 408 AA.
AC U3U2F0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=E05_36450 {ECO:0000313|EMBL:BAN98411.1};
OS Plautia stali symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN98411.1, ECO:0000313|Proteomes:UP000016901};
RN [1] {ECO:0000313|EMBL:BAN98411.1, ECO:0000313|Proteomes:UP000016901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT lipopolysaccharide.";
RL Microbiol. Res. 167:48-54(2011).
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}.
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DR EMBL; AP012551; BAN98411.1; -; Genomic_DNA.
DR AlphaFoldDB; U3U2F0; -.
DR MEROPS; M20.003; -.
DR KEGG; psts:E05_36450; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_053676_0_0_6; -.
DR Proteomes; UP000016901; 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 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:BAN98411.1}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00550};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00550};
KW Metal-binding {ECO:0000256|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:UP000016901};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 206..303
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 80
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-1"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT 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|HAMAP-Rule:MF_00550,
FT 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|HAMAP-Rule:MF_00550,
FT 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|HAMAP-Rule:MF_00550,
FT 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|HAMAP-Rule:MF_00550,
FT 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|HAMAP-Rule:MF_00550,
FT ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 379
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 408 AA; 44775 MW; EEB25DFCADF9A3DF CRC64;
MDQLLERFLS YVAVETQAKP QARQVPSSEG QWTLARQLQE ELIALGFVDV TLSDHCCVMG
TLPANVDWPT PVIGFISHMD TSPDFTAKNV NPQIIENYRG GDIALGNGDE VLSPVMFPVL
HKLTGHTLIT TDGKTLLGAD DKAGIAEIMT AMAELAKGNV PHGGIRLAFT PDEEIGRGTS
HFDVEGFAAD WAYTVDGSDL GEFEFENFNA ATALVKITGN NVHPGSAKNV MVNALDLAMR
FHAELPAKEK PQFTDGYEGF FHLHTIKGSV EHAELMYLIR DFDADSYEQR KQLLQEIGRR
VSKGLQAECS IKVEISDSYR NMREKVEPHP HIIELALQAM RDCGIEPNVK PIRGGTDGSA
LSWKGLPCPN LFTGGYNYHG KHEFASLNVM AKSVEVIVRL AALAAEKK
//
