ID A0A0M2HDP3_9MICO Unreviewed; 446 AA.
AC A0A0M2HDP3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:KJL44728.1};
DE EC=3.5.1.18 {ECO:0000313|EMBL:KJL44728.1};
GN Name=dapE_2 {ECO:0000313|EMBL:KJL44728.1};
GN ORFNames=RS82_00686 {ECO:0000313|EMBL:KJL44728.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL44728.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL44728.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL44728.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJL44728.1}.
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; JYJA01000024; KJL44728.1; -; Genomic_DNA.
DR RefSeq; WP_045296904.1; NZ_JYJA01000024.1.
DR AlphaFoldDB; A0A0M2HDP3; -.
DR PATRIC; fig|69370.6.peg.710; -.
DR OrthoDB; 3665926at2; -.
DR Proteomes; UP000034098; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.900; -; 1.
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; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KJL44728.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000034098};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 198..345
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 446 AA; 48273 MW; B28A7C33B591057C CRC64;
MSPADVAPRA GIAERLSRMI QLPTVSAERS ERGQGPFDAF ADLLIELYPL VHEHLERERI
GELGILYRWR GRIAERPTVL MAHFDVVPVD ESDAWTHPPF EGRVDRGWVY GRGSLDDKGP
LVVVMDAVEN LLASGFTPAR DVYLSFGGDE ETFGGAARTI AETLRDRGVA PWLVLDEGGA
VVDAPLPFVR GTAAMVGVGE KGVLTLRLSA RGEGGHASAP PARTAVRRIA RAVERLSPET
FPARTPAAVT RMLELFATRT GGISRALYRL LSRAPWLTAR AFTAMGGEPA ALVRTTVAAT
MQSGGTAANV LPSQATATLN LRIALGESVG STVKRVRKRV ADRHVKVEVL EGDGPSPESS
TENAQFALIT DAVKVSHPGA ATVPYVMMAA TDSRHFHRFS PAVYRFAPLE MSKAQRASIH
GVDERVEISA LERGELFHRT LLQRLE
//
