ID A0A0F0KE41_9MICO Unreviewed; 447 AA.
AC A0A0F0KE41;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:KJL19138.1};
DE EC=3.5.1.18 {ECO:0000313|EMBL:KJL19138.1};
GN Name=dapE_2 {ECO:0000313|EMBL:KJL19138.1};
GN ORFNames=RN50_02417 {ECO:0000313|EMBL:KJL19138.1};
OS Microbacterium foliorum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=104336 {ECO:0000313|EMBL:KJL19138.1, ECO:0000313|Proteomes:UP000033572};
RN [1] {ECO:0000313|EMBL:KJL19138.1, ECO:0000313|Proteomes:UP000033572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12966 {ECO:0000313|EMBL:KJL19138.1,
RC ECO:0000313|Proteomes:UP000033572};
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:KJL19138.1}.
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DR EMBL; JYIU01000045; KJL19138.1; -; Genomic_DNA.
DR RefSeq; WP_045254766.1; NZ_JYIU01000045.1.
DR AlphaFoldDB; A0A0F0KE41; -.
DR KEGG; mfol:DXT68_03570; -.
DR PATRIC; fig|104336.4.peg.2463; -.
DR Proteomes; UP000033572; 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:KJL19138.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000033572};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 199..345
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 447 AA; 47281 MW; E2A27B22E061BE0D CRC64;
MADVTAPRPG IAERLAQMIQ LPTVSAELAQ RGTGPFEDFA ALIAELYPLV HERLALERHT
EFGLLFHWTG SGAAPGGPVV LMAHYDVVPV DESDAWTHPP FAGVIADGLV HGRGALDDKG
PLLVVLEAVE NLLAEGVVPA RDVYLSFGGN EETYGDAARE IARTFRERGI VPWLVVDEGG
AVVDAPLPFV PGRAAMIGVG EKGLMTLTLS ARGDGGHASA PPTRTAVRRI ARAVDRLGPS
TFRPRPSRAI GRMLSQLGAQ TPGPAGLLLR LLGSARFLTG RLFAALGGES AALVRTTVAP
TMQSGGTASN VLPSQASATL NLRIALGETP QQAVLRVRRR IRDPLVTVRV EEASAPSPES
ATDNAQFALL AEALAVSHPG VAAVPYVMMA ATDSRHFHRF APAVYRFAPL EMSNAQRASI
HGVDENVEIS ALERGVMFYR ALILGLG
//
