DAPE_STAES
ID DAPE_STAES Reviewed; 405 AA.
AC Q8CQC2;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase;
DE Short=SDAP desuccinylase;
DE EC=3.5.1.18;
GN Name=dapE; OrderedLocusNames=SE_0216;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-
CC 2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609,
CC ChEBI:CHEBI:58087; EC=3.5.1.18;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (succinylase route): step 3/3.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AE015929; AAO03813.1; -; Genomic_DNA.
DR RefSeq; NP_763771.1; NC_004461.1.
DR RefSeq; WP_002485521.1; NZ_WBME01000011.1.
DR AlphaFoldDB; Q8CQC2; -.
DR SMR; Q8CQC2; -.
DR STRING; 176280.SE_0216; -.
DR EnsemblBacteria; AAO03813; AAO03813; SE_0216.
DR KEGG; sep:SE_0216; -.
DR PATRIC; fig|176280.10.peg.195; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_2_9; -.
DR OMA; NCDVDGF; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000001411; Chromosome.
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:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR InterPro; IPR010182; ArgE/DapE.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01910; DapE-ArgE; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cobalt; Diaminopimelate biosynthesis; Hydrolase;
KW Lysine biosynthesis; Metal-binding; Zinc.
FT CHAIN 1..405
FT /note="Probable succinyl-diaminopimelate desuccinylase"
FT /id="PRO_0000185269"
FT ACT_SITE 74
FT /evidence="ECO:0000250"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 405 AA; 44973 MW; D70A3449C0BBE3E6 CRC64;
MTVLSEQDKI RLLADIVKIQ TENDHEIEVC EYLKDLLSQY DIDSKIVKVN DSRANLVAEI
GSGAPVLAIS GHMDVVDAGD HDDWTFPPFE LTDKDGKLFG RGTTDMKGGL MAMVIAMIEL
KQSNALKQGT IRLLATTGEE TEQYGAQLLA DEGYLDDVSG LIIGEPTSNI AYYAHKGSMS
CVVTAKGKAA HSSMPHLGTN AVDILVDFVN EMKQEYKNIK EHDKVHELDA VPMIEKHLHR
KIGEEESHIY SGFVMLNSVF NGGKQVNSVP HKATAKYNVR TVPEYDSTFV KDLFEKVIRH
VGENYLTVDI PSSHDPVASD RDNPLIQNIT RIAPNYVHED IVVSALIGTT DASSFLGTNE
NNVDFAVFGP GESIMAHQVD EFIRKDMYLS YIDVYKDVFK AYLEK
