ID   DAPEL_BACSU             Reviewed;         374 AA.
AC   O34916; Q796K0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=ykuR; Synonyms=dapL; OrderedLocusNames=BSU14190;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Scanlan E., Devine K.M.;
RT   "Sequence of the Bacillus subtilis chromosome from ykuA to cse-15.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION AS A N-ACETYLDIAMINOPIMELATE DEACETYLASE AND IN DIAMINOPIMELATE
RP   BIOSYNTHESIS.
RC   STRAIN=168;
RX   PubMed=5411754; DOI=10.1128/jb.101.1.323-324.1970;
RA   Weinberger S., Gilvarg C.;
RT   "Bacterial distribution of the use of succinyl and acetyl blocking groups
RT   in diaminopimelic acid biosynthesis.";
RL   J. Bacteriol. 101:323-324(1970).
CC   -!- FUNCTION: Catalyzes the conversion of N-acetyl-diaminopimelate to
CC       diaminopimelate and acetate. {ECO:0000255|HAMAP-Rule:MF_01692,
CC       ECO:0000269|PubMed:5411754}.
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; AJ222587; CAA10881.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13292.1; -; Genomic_DNA.
DR   PIR; G69866; G69866.
DR   RefSeq; NP_389302.1; NC_000964.3.
DR   RefSeq; WP_003232383.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34916; -.
DR   SMR; O34916; -.
DR   STRING; 224308.BSU14190; -.
DR   MEROPS; M20.A27; -.
DR   PaxDb; O34916; -.
DR   PRIDE; O34916; -.
DR   EnsemblBacteria; CAB13292; CAB13292; BSU_14190.
DR   GeneID; 938805; -.
DR   KEGG; bsu:BSU14190; -.
DR   PATRIC; fig|224308.179.peg.1548; -.
DR   eggNOG; COG1473; Bacteria.
DR   InParanoid; O34916; -.
DR   OMA; RAHACGH; -.
DR   PhylomeDB; O34916; -.
DR   BioCyc; BSUB:BSU14190-MON; -.
DR   UniPathway; UPA00034; UER00024.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR   GO; GO:0050118; F:N-acetyldiaminopimelate deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Diaminopimelate biosynthesis; Hydrolase;
KW   Lysine biosynthesis; Reference proteome.
FT   CHAIN           1..374
FT                   /note="N-acetyldiaminopimelate deacetylase"
FT                   /id="PRO_0000360658"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
FT   ACT_SITE        128
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01692"
SQ   SEQUENCE   374 AA;  41557 MW;  56E3BF815C993D3D CRC64;
     MKIEELIAIR RDLHRIPELG FQEFKTQQYL LNVLEQYPQD RIEIEKWRTG LFVKVNGTAP
     EKMLAYRADI DALSIEEQTG LPFASEHHGN MHACGHDLHM TIALGIIDHF VHHPVKHDLL
     FLFQPAEEGP GGAEPMLESD VLKKWQPDFI TALHIAPELP VGTIATKSGL LFANTSELVI
     DLEGKGGHAA YPHLAEDMVV AASTLVTQLQ TIISRNTDPL DSAVITVGTI TGGSAQNIIA
     ETAHLEGTIR TLSEESMKQV KERIEDVVKG IEIGFRCKGK VTYPSVYHQV YNTSGLTEEF
     MSFVAEHQLA TVIEAKEAMT GEDFGYMLKK YPGFMFWLGA DSEHGLHHAK LNPDENAIET
     AVHVMTGYFS VYAN