ID A0A0Q5JVV4_9MICO Unreviewed; 358 AA.
AC A0A0Q5JVV4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:KQR24938.1};
DE EC=3.5.1.18 {ECO:0000313|EMBL:KQR24938.1};
GN ORFNames=ASF76_04510 {ECO:0000313|EMBL:KQR24938.1};
OS Microbacterium sp. Leaf151.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736276 {ECO:0000313|EMBL:KQR24938.1, ECO:0000313|Proteomes:UP000051582};
RN [1] {ECO:0000313|EMBL:KQR24938.1, ECO:0000313|Proteomes:UP000051582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf151 {ECO:0000313|EMBL:KQR24938.1,
RC ECO:0000313|Proteomes:UP000051582};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR24938.1, ECO:0000313|Proteomes:UP000051582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf151 {ECO:0000313|EMBL:KQR24938.1,
RC ECO:0000313|Proteomes:UP000051582};
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:KQR24938.1}.
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DR EMBL; LMOR01000002; KQR24938.1; -; Genomic_DNA.
DR RefSeq; WP_055953671.1; NZ_LMOR01000002.1.
DR AlphaFoldDB; A0A0Q5JVV4; -.
DR STRING; 1736276.ASF76_04510; -.
DR OrthoDB; 7055905at2; -.
DR Proteomes; UP000051582; 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:KQR24938.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 171..267
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 358 AA; 38540 MW; C90A5A12E8B6B025 CRC64;
MPVLDLTASS VDLTRAICDI PSVSDDETPL ADAIEAAVSA YDHLEVIRDG DTIVARTSLG
RSRRVVIAGH IDTVPINRNL PVEDREIDGQ AFLWGRGTVD MKAGVAVQLK LAAELTDPAV
DITWMWYDHE EVDSTLNGLG RLSRNRPDLF EGDFAILGEP SNGEVEGGCN GTLRALIRTD
GVRAHSARSW IGENAIHKAA PILARLAEYR AREIEVEGLV YREGLNAVRI SGGVAGNVIP
DACEVEVNYR FAPSRDAEGA ARVVRDVFTG FEVDIVDIAE GARPGLDAPL AKEFVDAVGA
TPTPKYGWTD VARFSALGIP AVNYGPGDPH LAHHDEERVP VAQIDAVERG LRAWLSAS
//
