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Database: UniProt
Entry: A0A120FK54_9BRAD
LinkDB: A0A120FK54_9BRAD
Original site: A0A120FK54_9BRAD 
ID   A0A120FK54_9BRAD        Unreviewed;       418 AA.
AC   A0A120FK54;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peptidase T {ECO:0000313|EMBL:KWV50166.1};
DE            EC=3.4.11.4 {ECO:0000313|EMBL:KWV50166.1};
GN   ORFNames=AS156_14460 {ECO:0000313|EMBL:KWV50166.1};
OS   Bradyrhizobium macuxiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV50166.1, ECO:0000313|Proteomes:UP000057737};
RN   [1] {ECO:0000313|EMBL:KWV50166.1, ECO:0000313|Proteomes:UP000057737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR 10303 {ECO:0000313|EMBL:KWV50166.1,
RC   ECO:0000313|Proteomes:UP000057737};
RA   Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT   "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT   from nodules of Centrolobium paraense.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR037215-2};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR037215-
CC       2};
CC   -!- SIMILARITY: Belongs to the peptidase M20B family.
CC       {ECO:0000256|ARBA:ARBA00009692}.
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:KWV50166.1}.
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DR   EMBL; LNCU01000096; KWV50166.1; -; Genomic_DNA.
DR   RefSeq; WP_066511765.1; NZ_LNCU01000096.1.
DR   AlphaFoldDB; A0A120FK54; -.
DR   OrthoDB; 9804934at2; -.
DR   Proteomes; UP000057737; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03892; M20_peptT; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 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; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:KWV50166.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KWV50166.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR037215-2};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT   DOMAIN          218..316
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT   BINDING         389
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
SQ   SEQUENCE   418 AA;  45762 MW;  87FF307167CD4B67 CRC64;
     MLAPVLDFKH TVTERFLRYV VIDTQSDPDS PTCPSTEKQK NLGRLLVSEL QAMGISDAHL
     DAHGYVYATI RANTEKTVPV ICFCSHMDTS PDCTGKDVKP QIVTNYRGGD LVLPADPSQV
     IRAAEHEALA DQIGNDIITT DGTTLLGADN KAGLAEIMDA AHFLITNPQL KHGTIKILFT
     PDEEIGRGVD KVDIKKLGAD FGYTMDGESA GHIEDETFSA DGASIMIEGV ATHPGFAKGK
     MEHAIKIAAA IVDRLPKDAC SPETTEGKEG FLHPVAISGA LEKARIDFIV RDFAEAGLKQ
     KEALLEGIVK DVMKAYPRST YRLEVREQYR NMKEVIDRHP EVVAYAIEAI KRAGLSPVKT
     SIRGGTDGSR LSFMGLPCPN IFAGEHAFHS RLEWVSRQDM EKAVQTIVHL AMIWEERA
//
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