PEPT_EDWI9
ID PEPT_EDWI9 Reviewed; 412 AA.
AC C5BFN3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=NT01EI_1819;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001600; ACR68996.1; -; Genomic_DNA.
DR RefSeq; WP_015871142.1; NC_012779.2.
DR AlphaFoldDB; C5BFN3; -.
DR SMR; C5BFN3; -.
DR STRING; 67780.B6E78_02185; -.
DR MEROPS; M20.003; -.
DR EnsemblBacteria; ACR68996; ACR68996; NT01EI_1819.
DR GeneID; 7962140; -.
DR KEGG; eic:NT01EI_1819; -.
DR PATRIC; fig|634503.3.peg.1632; -.
DR HOGENOM; CLU_053676_0_0_6; -.
DR OMA; GHNFHGK; -.
DR OrthoDB; 1015417at2; -.
DR Proteomes; UP000001485; 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..412
FT /note="Peptidase T"
FT /id="PRO_1000211991"
FT ACT_SITE 80
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 78
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 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT BINDING 196
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 412 AA; 44584 MW; 8625F30599C929F2 CRC64;
MNNLLDRFLN YVSFDTQSKP GVRQVPSTEG QFRLARALQS ELLALGLEQV TLSEHGCVMA
TLPANVAWPV PTIGFIAHMD TAPDASGKNV NPQIVENYRG GDIALGIGDE ILSPVMFPVL
HQLLGQTLIT TDGKTLLGAD DKSGIAEIMT AMVRLKQGNT PHGEIRVAFT PDEEVGKGAQ
HFDVAAFGAE WAYTVDGGGV GELECENFNA ASVNIKIIGN NVHPGSAKGV MVNALGLANR
IHALLPAAEV PEQTDGYEGF YHLVSMKGSV EKAEMHYIVR DFSREGFEAR KKHMMAIAKQ
VGQGLHPDCY IEVTLDDSYY NMRDEVAKHP HIVALARQAM CDLAIEPIER PIRGGTDGAQ
LSFHGLPCPN LFTGGYNFHG KHEFITLEGM EKAVSVIMRI AELTAGRARV AG
