ID A0A0Q1E357_9CORY Unreviewed; 440 AA.
AC A0A0Q1E357;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:KQB87092.1};
DE EC=3.5.1.18 {ECO:0000313|EMBL:KQB87092.1};
GN Name=dapE_1 {ECO:0000313|EMBL:KQB87092.1};
GN ORFNames=Clow_00140 {ECO:0000313|EMBL:KQB87092.1};
OS Corynebacterium lowii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB87092.1, ECO:0000313|Proteomes:UP000050488};
RN [1] {ECO:0000313|EMBL:KQB87092.1, ECO:0000313|Proteomes:UP000050488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130206 {ECO:0000313|EMBL:KQB87092.1,
RC ECO:0000313|Proteomes:UP000050488};
RA Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S.,
RA Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H.,
RA Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.;
RT "Corynebacteirum lowii and Corynebacterium oculi species nova, derived from
RT human clinical disease and and emended description of Corynebacterium
RT mastiditis.";
RL Submitted (OCT-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:KQB87092.1}.
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DR EMBL; LKEV01000001; KQB87092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q1E357; -.
DR STRING; 1544413.Clow_00140; -.
DR PATRIC; fig|1544413.3.peg.143; -.
DR Proteomes; UP000050488; 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 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; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF32; CONSERVED 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:KQB87092.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050488}.
FT DOMAIN 190..333
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 440 AA; 47394 MW; 21A5F0AC4E832A45 CRC64;
MSLYDDTLAL LQELIRNACV NDLTADSGQE IRNVESLERF FAGSGVAVRR FEPHPGRTSI
AFSVEGSDPA AEPLTLLGHI DVVPVDEPQW SVPPFGAEII DGKIYGRGAM DMLFITATMA
AVTREVARAG GARGTLTFVA LADEEARGGL GAGWIAQHEP EAFSWRNCLS ETGGSHLPTA
DSSDAVVINV GEKGAAQRRL HVTGDAGHGS TPHGKDSAIV KIGEVARRIA AAEPPVTDNA
VWRGFVQAFR FDPATEHALL DGTGNYEVFG DLAAYAQAFS HNTFAQTALR AGGPINVLPS
HAWLDMDIRP LPGTTQEAID AVLREALGDL AEQVRIEHLI TEPATESPAS GPLWEAMVET
IHEEFPQAEV VPVLATGGSD LRFARRLGGV GYGFALHARE RTLAEANKQL HSHDEHLHLE
DLRLTVHAYR RLVRRFLGVL
//
