ID   A0A086ZET4_9BIFI        Unreviewed;       411 AA.
AC   A0A086ZET4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:KFI45034.1};
DE            EC=3.5.1.18 {ECO:0000313|EMBL:KFI45034.1};
GN   ORFNames=BBOH_1294 {ECO:0000313|EMBL:KFI45034.1};
OS   Bifidobacterium bohemicum DSM 22767.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437606 {ECO:0000313|EMBL:KFI45034.1, ECO:0000313|Proteomes:UP000029096};
RN   [1] {ECO:0000313|EMBL:KFI45034.1, ECO:0000313|Proteomes:UP000029096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22767 {ECO:0000313|EMBL:KFI45034.1,
RC   ECO:0000313|Proteomes:UP000029096};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) 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:KFI45034.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JGYP01000004; KFI45034.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A086ZET4; -.
DR   STRING; 1437606.BBOH_1294; -.
DR   eggNOG; COG0624; Bacteria.
DR   Proteomes; UP000029096; 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:KFI45034.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029096}.
FT   DOMAIN          205..296
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   411 AA;  44246 MW;  19B2CA2B3F4D181F CRC64;
     MRTNAAWRAR PGYDGGMTLV IEPGAERPQV LADLFGALMR VHSVSDEERA IADDVEAFLN
     AQPHLDVRRM GDTVVASTSL GRPQRVVLAG HLDTVPALGN FPPRWLEPDD PQVRDDVRTA
     HPGERVMFGR GAVDMKGSDA VMLYLAATLT DPKYDLTFVF YDHEEVAAEK NGLFRVATAH
     PDWIQGDFAI IGEPTDCGIE GGCNGTMRFD VVTHGIAAHS ARAWMGDNAI HKAADVLNRL
     ASYEPQDVEV DGLVYREGVN ATLISGGSGT NIIPDQCRVH VNYRFAPDKS IEAAKTLMMG
     SDTGAELGNG EHTATGGMFE GFGIEMKDES PSARPGMDSP LAVSLASLVR ERTGRVPLAK
     LGWTDVARFS SIGVPAVNLG AGSPLLAHKA DEQLPEGELE LLADILIRWL S
//