ID   DAPH_STRSY              Reviewed;         232 AA.
AC   A4VY24; A4VY22;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase;
DE            EC=2.3.1.89;
DE   AltName: Full=Tetrahydrodipicolinate N-acetyltransferase;
DE            Short=THP acetyltransferase;
DE            Short=Tetrahydropicolinate acetylase;
GN   Name=dapH; OrderedLocusNames=SSU05_2046/SSU05_2047;
OS   Streptococcus suis (strain 05ZYH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05ZYH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(2007).
CC   -!- FUNCTION: Catalyzes the transfer of an acetyl group from acetyl-CoA to
CC       tetrahydrodipicolinate. {ECO:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (acetylase route): step 1/3.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. DapH
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABP91011.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=ABP91012.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000407; ABP91012.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CP000407; ABP91011.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; A4VY24; -.
DR   SMR; A4VY24; -.
DR   STRING; 391295.SSU05_2047; -.
DR   EnsemblBacteria; ABP91011; ABP91011; SSU05_2046.
DR   EnsemblBacteria; ABP91012; ABP91012; SSU05_2047.
DR   KEGG; ssu:SSU05_2046; -.
DR   KEGG; ssu:SSU05_2047; -.
DR   eggNOG; COG2171; Bacteria.
DR   HOGENOM; CLU_2193712_0_0_9; -.
DR   UniPathway; UPA00034; UER00022.
DR   Proteomes; UP000000243; 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; 2.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR03532; DapD_Ac; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Diaminopimelate biosynthesis;
KW   Lysine biosynthesis; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..232
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   acetyltransferase"
FT                   /id="PRO_0000376717"
SQ   SEQUENCE   232 AA;  23891 MW;  A8EC9403F74474E0 CRC64;
     MTAQKMTAQE IIAFIGNAVK KTTVKVTFEG ELAGAVPAEV TKLGNVLFGD WKDVEPLLAN
     LTENVDYVVE QDGRNSAVPL LDKRNINARI EPGAIIRDQV TIGDNAVIMM GAVINIGAEI
     GPGTMIDMGA ILGGRATVGK NSHIGAGAVL AGVIEPASAE PVRVGDNVLV GANAVVIEGV
     QIGSGSVVAA GAIVTQDVPE NVVVAGVPAR IIKEIDAQTQ QKTALEEALR TL