ID   A0A0Q8UZT4_9MICO        Unreviewed;       360 AA.
AC   A0A0Q8UZT4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:KRC50628.1};
DE            EC=3.5.1.18 {ECO:0000313|EMBL:KRC50628.1};
GN   ORFNames=ASE16_06365 {ECO:0000313|EMBL:KRC50628.1};
OS   Leifsonia sp. Root227.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736496 {ECO:0000313|EMBL:KRC50628.1, ECO:0000313|Proteomes:UP000051819};
RN   [1] {ECO:0000313|EMBL:KRC50628.1, ECO:0000313|Proteomes:UP000051819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root227 {ECO:0000313|EMBL:KRC50628.1,
RC   ECO:0000313|Proteomes:UP000051819};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC50628.1, ECO:0000313|Proteomes:UP000051819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root227 {ECO:0000313|EMBL:KRC50628.1,
RC   ECO:0000313|Proteomes:UP000051819};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KRC50628.1}.
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DR   EMBL; LMIO01000002; KRC50628.1; -; Genomic_DNA.
DR   RefSeq; WP_055892456.1; NZ_LMIO01000002.1.
DR   AlphaFoldDB; A0A0Q8UZT4; -.
DR   STRING; 1736496.ASE16_06365; -.
DR   OrthoDB; 7055905at2; -.
DR   Proteomes; UP000051819; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR010174; Succinyl-DAP_deSuclase_DapE.
DR   NCBIfam; TIGR01900; dapE-gram_pos; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KRC50628.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051819}.
FT   DOMAIN          170..268
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   360 AA;  38757 MW;  AE592FD08820DB88 CRC64;
     MPLDLSASSI DITRQICDIE SVSGNEKELA DAIVEALSGL GHLEIIRDGD TVVARTNLGR
     DRRAVIAGHI DTVPLNDNLP TRFETIDGIQ YLWGRGTVDM KSGTAVQLKL AAELTDPAID
     ITWMWYDHEE VSADLNGLGR LARNRPDLFE GDFAILGEPS NGVVEGGCNG NLRVEVRTYG
     LRAHSARGWI GENAIHKATP ILDTLAAYQA REVEVDGLVY REGLNAVGIS GGVAGNIIPD
     ECMVHINYRF APSRSSEDAI AHMHELFGDY EITVVDRADG ARPGLDAPLA QEFLAAVGGV
     AKPKYGWTDV ARFSAMGIPA VNYGPGDPLK AHADDERVAV DQITAVEAGL RAWLTGAPRR
//