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Database: UniProt
Entry: J3CGC5_9FLAO
LinkDB: J3CGC5_9FLAO
Original site: J3CGC5_9FLAO 
ID   J3CGC5_9FLAO            Unreviewed;       415 AA.
AC   J3CGC5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=PMI13_02708 {ECO:0000313|EMBL:EJL70846.1};
OS   Chryseobacterium populi.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1144316 {ECO:0000313|EMBL:EJL70846.1, ECO:0000313|Proteomes:UP000007509};
RN   [1] {ECO:0000313|EMBL:EJL70846.1, ECO:0000313|Proteomes:UP000007509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF314 {ECO:0000313|EMBL:EJL70846.1,
RC   ECO:0000313|Proteomes:UP000007509};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJL70846.1}.
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DR   EMBL; AKJY01000050; EJL70846.1; -; Genomic_DNA.
DR   RefSeq; WP_007844503.1; NZ_AKJY01000050.1.
DR   AlphaFoldDB; J3CGC5; -.
DR   MEROPS; M20.003; -.
DR   PATRIC; fig|1144316.3.peg.2726; -.
DR   OrthoDB; 9804934at2; -.
DR   Proteomes; UP000007509; 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   Zinc {ECO:0000256|HAMAP-Rule:MF_00550, ECO:0000256|PIRSR:PIRSR037215-2}.
FT   DOMAIN          218..315
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT                   ECO:0000256|PIRSR:PIRSR037215-1"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00550,
FT                   ECO:0000256|PIRSR:PIRSR037215-1"
FT   BINDING         89
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         152
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         152
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         187
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         209
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         391
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   415 AA;  45939 MW;  9F4F198D6C5DDEE1 CRC64;
     MSTIEFTPLW KEKLLNRFLN YVKIYSTSDA ESEATPSTPQ QWDIAKYIVE ELKTIGLEGV
     SIDDNGYIIG YVPSNIENDE RPTIGFISHY DTSPDFSGEN VKPQVWENYA GDDLILNQTT
     GFTLSPSKFE SLKKYIGQTL ITTDGNTLLG ADDKAGCAEI VTAAEYLIAH PEIKHGRIAI
     GFTPDEEIGR GAHKFDVAKF GAEWAYTMDG GEVGELEYEN FNAAGAVVKI HGLSVHPGYA
     YGKMVNAALL ASEFAQMLPA NETPATTKGF DGFYHLMEIT ADISEAKLQY IIRDHDEEKF
     EARKKLMEEK VAEFNQKHGA GTADVEIKEQ YRNMKQQFEG KMHIIDLAAK AMQEANIEPK
     IKAIRGGTDG AQLSYMGLPC PNIFAGGINF HGPYEYVALE SMEKATEVII NIVKA
//
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