ID   DAPEL_LACLA             Reviewed;         384 AA.
AC   Q9CIS4;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=N-acetyldiaminopimelate deacetylase {ECO:0000255|HAMAP-Rule:MF_01692};
DE            EC=3.5.1.47 {ECO:0000255|HAMAP-Rule:MF_01692};
GN   Name=yciA; Synonyms=dapL; OrderedLocusNames=LL0282; ORFNames=L80177;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Catalyzes the conversion of N-acetyl-diaminopimelate to
CC       diaminopimelate and acetate. {ECO:0000255|HAMAP-Rule:MF_01692}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-
CC         diaminoheptanedioate + acetate; Xref=Rhea:RHEA:20405,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57609,
CC         ChEBI:CHEBI:58767; EC=3.5.1.47; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01692};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (acetylase route): step 3/3. {ECO:0000255|HAMAP-Rule:MF_01692}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. N-
CC       acetyldiaminopimelate deacetylase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01692}.
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DR   EMBL; AE005176; AAK04380.1; -; Genomic_DNA.
DR   PIR; B86660; B86660.
DR   RefSeq; NP_266438.1; NC_002662.1.
DR   RefSeq; WP_010905261.1; NC_002662.1.
DR   AlphaFoldDB; Q9CIS4; -.
DR   SMR; Q9CIS4; -.
DR   STRING; 272623.L80177; -.
DR   PaxDb; Q9CIS4; -.
DR   EnsemblBacteria; AAK04380; AAK04380; L80177.
DR   KEGG; lla:L80177; -.
DR   PATRIC; fig|272623.7.peg.309; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_0_1_9; -.
DR   OMA; RAHACGH; -.
DR   UniPathway; UPA00034; UER00024.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0050118; F:N-acetyldiaminopimelate deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01692; DapEL; 1.
DR   InterPro; IPR023905; AcetylDAP_deacetylase.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR11014; PTHR11014; 1.
DR   PANTHER; PTHR11014:SF98; PTHR11014:SF98; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Diaminopimelate biosynthesis; Hydrolase;
KW   Lysine biosynthesis; Reference proteome.
FT   CHAIN           1..384
FT                   /note="N-acetyldiaminopimelate deacetylase"
FT                   /id="PRO_0000376768"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ   SEQUENCE   384 AA;  43100 MW;  1E3A34BF39BAFA8E CRC64;
     MINLIEIRRQ LHQIPEIGLE EYETQKYLLA IIQELTQNKP FIQVRTWQTG ILVYLAGSQS
     QKTIGWRTDI DGLPIEELTD LPYASKNGRM HACGHDIHMT VALGLLEKMS ESQPRDNLLF
     LFQPAEENEA GGKLMYDARA FENWLPDEFY GLHVRPDLKV GDIATNQHTL FAGTCEVELS
     FIGTGGHAAF PHTANDALVA AAYFITQVQT IVSRNVDPLA SAVVTFGKME AGTTNNIIAE
     RAFLHGTIRS LTQEVNELTQ KRLRELANGI AQSFNMEIEL KLKQGGYLPV ENHPKLAKEL
     MEFFKKETKA NLIDIAPAMT GEDFGYLLSK IPGVMFWLGI DSDAPLHSQK MNPDEHVLNF
     SVDTISQFLQ FKVNRLSEGE KTIN