ID   DAPH_STAAM              Reviewed;         239 AA.
AC   Q7A2S0;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01691};
DE            EC=2.3.1.89 {ECO:0000255|HAMAP-Rule:MF_01691};
DE   AltName: Full=Tetrahydrodipicolinate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01691};
DE            Short=THP acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01691};
DE            Short=Tetrahydropicolinate acetylase {ECO:0000255|HAMAP-Rule:MF_01691};
GN   Name=dapH {ECO:0000255|HAMAP-Rule:MF_01691}; OrderedLocusNames=SAV1397;
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   -!- FUNCTION: Catalyzes the transfer of an acetyl group from acetyl-CoA to
CC       tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_01691}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + acetyl-CoA + H2O = CoA +
CC         L-2-acetamido-6-oxoheptanedioate; Xref=Rhea:RHEA:13085,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16845, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:58117; EC=2.3.1.89;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01691};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (acetylase route): step 1/3. {ECO:0000255|HAMAP-Rule:MF_01691}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. DapH
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01691}.
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DR   EMBL; BA000017; BAB57559.1; -; Genomic_DNA.
DR   RefSeq; WP_000249839.1; NC_002758.2.
DR   PDB; 3BV8; X-ray; 1.75 A; A=5-88.
DR   PDBsum; 3BV8; -.
DR   AlphaFoldDB; Q7A2S0; -.
DR   SMR; Q7A2S0; -.
DR   PaxDb; Q7A2S0; -.
DR   EnsemblBacteria; BAB57559; BAB57559; SAV1397.
DR   KEGG; sav:SAV1397; -.
DR   HOGENOM; CLU_103751_0_0_9; -.
DR   OMA; HLEYDRR; -.
DR   PhylomeDB; Q7A2S0; -.
DR   BioCyc; SAUR158878:SAV_RS07525-MON; -.
DR   UniPathway; UPA00034; UER00022.
DR   EvolutionaryTrace; Q7A2S0; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0047200; F:tetrahydrodipicolinate N-acetyltransferase activity; IEA:UniProtKB-EC.
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_01691; DapH; 1.
DR   InterPro; IPR019873; DapH.
DR   InterPro; IPR013710; DapH_N.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF08503; DapH_N; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR03532; DapD_Ac; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Amino-acid biosynthesis;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; Repeat; Transferase.
FT   CHAIN           1..239
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   acetyltransferase"
FT                   /id="PRO_0000376694"
FT   HELIX           7..17
FT                   /evidence="ECO:0007829|PDB:3BV8"
FT   STRAND          22..29
FT                   /evidence="ECO:0007829|PDB:3BV8"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:3BV8"
FT   STRAND          48..54
FT                   /evidence="ECO:0007829|PDB:3BV8"
FT   HELIX           55..65
FT                   /evidence="ECO:0007829|PDB:3BV8"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:3BV8"
FT   STRAND          69..76
FT                   /evidence="ECO:0007829|PDB:3BV8"
FT   HELIX           78..81
FT                   /evidence="ECO:0007829|PDB:3BV8"
SQ   SEQUENCE   239 AA;  25258 MW;  D7E6F32A2612525E CRC64;
     MVQHLTAEEI IQYISDAKKS TPIKVYLNGN FEGITYPESF KVFGSEQSKV IFCEADDWKP
     FYEAYGSQFE DIEIEMDRRN SAIPLKDLTN TNARIEPGAF IREQAIIEDG AVVMMGATIN
     IGAVVGEGTM IDMNATLGGR ATTGKNVHVG AGAVLAGVIE PPSASPVIIE DDVLIGANAV
     ILEGVRVGKG AIVAAGAIVT QDVPAGAVVA GTPAKVIKQA SEVQDTKKEI VAALRKLND