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Database: UniProt
Entry: A0A2V5KBB8_9BACL
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ID   A0A2V5KBB8_9BACL        Unreviewed;       416 AA.
AC   A0A2V5KBB8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN   ORFNames=DLM86_04335 {ECO:0000313|EMBL:PYI56222.1};
OS   Paenibacillus flagellatus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2211139 {ECO:0000313|EMBL:PYI56222.1, ECO:0000313|Proteomes:UP000247476};
RN   [1] {ECO:0000313|EMBL:PYI56222.1, ECO:0000313|Proteomes:UP000247476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DXL2 {ECO:0000313|EMBL:PYI56222.1,
RC   ECO:0000313|Proteomes:UP000247476};
RA   Dai X.;
RT   "Paenibacillus flagellatus sp. nov., isolated from selenium mineral soil.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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:PYI56222.1}.
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DR   EMBL; QJVJ01000002; PYI56222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5KBB8; -.
DR   OrthoDB; 9792335at2; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000247476; 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:UniProtKB-UniPathway.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR010182; ArgE/DapE.
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   NCBIfam; TIGR01910; DapE-ArgE; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 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.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247476};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          186..314
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   416 AA;  45341 MW;  47187F7ED7A1CF6D CRC64;
     MDWNKRLLEE IDKRQDELID LCSKLIQFPS ENPPGDTRDI SKFIIDYLQE AGIGTDVHES
     APNMLNLLST IGAEGEKHLL FCGHTDVVPA GDLSRWDFPP FGGLVRDGYI LGRGASDMKC
     GLAGLIFATA LLKRLGVPLA GQLSLFIVPD EETGGHYGVP WVLERGLITG TAAVIAEPSS
     PQHPTIGQKG SAWFEFTVEG TPGHGSLSPF KGDSAILKAA KAIEALQKLT EMKPTIPADV
     QEMIDISKEY ARKREVLDVS DVYDHVTVNI GTIHGGTKAN VVADKCTVEV DSRVPFGIDY
     RDVLAEAKRL LLEVGVDVEL KPIGFRANAN WTPPTEDIVK LLVESITDVN GQEAYGVLQW
     ATSDARHFRN HGIPVLQYGP AELSTIHNFN ERAPIDQVVQ AAKVYALTAL KYLGVK
//
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