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Database: UniProt
Entry: A0A0S9CNB2_9MICC
LinkDB: A0A0S9CNB2_9MICC
Original site: A0A0S9CNB2_9MICC 
ID   A0A0S9CNB2_9MICC        Unreviewed;       374 AA.
AC   A0A0S9CNB2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:KQN95130.1};
DE            EC=3.5.1.18 {ECO:0000313|EMBL:KQN95130.1};
GN   ORFNames=ASE96_02790 {ECO:0000313|EMBL:KQN95130.1};
OS   Arthrobacter sp. Leaf69.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN95130.1, ECO:0000313|Proteomes:UP000051467};
RN   [1] {ECO:0000313|EMBL:KQN95130.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN95130.1,
RC   ECO:0000313|Proteomes:UP000051467};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN95130.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN95130.1,
RC   ECO:0000313|Proteomes:UP000051467};
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   -!- 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:KQN95130.1}.
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DR   EMBL; LMLR01000001; KQN95130.1; -; Genomic_DNA.
DR   RefSeq; WP_056425611.1; NZ_LMLR01000001.1.
DR   AlphaFoldDB; A0A0S9CNB2; -.
DR   STRING; 1736232.ASE96_02790; -.
DR   OrthoDB; 7055905at2; -.
DR   Proteomes; UP000051467; Unassembled WGS sequence.
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:SF31; DIPEPTIDASE YTJP-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.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KQN95130.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          188..286
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   374 AA;  39579 MW;  DD0980623F97B55A CRC64;
     MTEHTAPARL DLRQDVALLT ADIIDIFSVS GEERRLADAV EHALRSVPQL EVVRDGDSII
     ARTNLGRAER VILAGHLDTV PLPTTEGSLG TVPSYWPSGA PGEGILYGRG ATDMKGGVAV
     QLALAAGLFD GGAEPDKDIT FVFYDHEEVE AVKSGLGRLV RNHGGLLGGD FAILLEPTNG
     TVEGGCNGTI RFEATTTGEA AHSARAWMGS NAIHAAAPIL ARLAAYEPRT ISVDGLDYRE
     SLNAVKVNGG TAGNVIPDRC VVEINYRFAP DKTPDEAERH VRELLEGFDV VRTDSAAGAR
     PGLTHPAAAS FVAAVGAAPK PKYGWTDVAR FSELGIPAVN FGPGDALLAH KDNEHVDADA
     IRDCLRALRS WLTE
//
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