ID   DAPE_STAAM              Reviewed;         400 AA.
AC   Q931I4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Probable succinyl-diaminopimelate desuccinylase;
DE            Short=SDAP desuccinylase;
DE            EC=3.5.1.18;
GN   Name=dapE; OrderedLocusNames=SAV2006;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB58168.1; -; Genomic_DNA.
DR   RefSeq; WP_000206624.1; NC_002758.2.
DR   AlphaFoldDB; Q931I4; -.
DR   SMR; Q931I4; -.
DR   PaxDb; Q931I4; -.
DR   EnsemblBacteria; BAB58168; BAB58168; SAV2006.
DR   KEGG; sav:SAV2006; -.
DR   HOGENOM; CLU_021802_2_2_9; -.
DR   OMA; CAHQPGE; -.
DR   PhylomeDB; Q931I4; -.
DR   BioCyc; SAUR158878:SAV_RS10965-MON; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000002481; 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..400
FT                   /note="Probable succinyl-diaminopimelate desuccinylase"
FT                   /id="PRO_0000185264"
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         378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  43995 MW;  AA2404D68491300D CRC64;
     MTTFSEKEKI QLLADIVELQ TENNNEIDVC NYLKDLFDKY DIKSEILKVN EHRANIVAEI
     GNGSPILALS GHMDVVDAGN QDNWTYPPFQ LTEKAGKLYG RGTTDMKGGL MALVITLIEL
     KEQNQLPQGT IRLLATAGEE KEQEGAKLLA DKGYLDDVDG LIIAEPTGSG IYYAHKGSMS
     CKVTATGKAV HSSVPFIGDN AIDTLLEFYN QFKEKYSELK KHDTKHELDV APMFKSLIGK
     EISEEDANYA SGLTAVCSII NGGKQFNSVP DEASLEFNVR PVPEYDNDFI ESFFQNIIND
     VDSNKLSLDI PSNHRPVTSD KNSKLITTIK DVASSYVEQD EIFVSALVGA TDASSFLGDN
     KDNVDLAIFG PGNPLMAHQI DEYCLTVNIQ ISTSTFSLIK