ID   THGA_LACLA              Reviewed;         207 AA.
AC   P52984; Q9CE64;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Galactoside O-acetyltransferase;
DE            Short=GAT;
DE            EC=2.3.1.18 {ECO:0000250|UniProtKB:P07464};
DE   AltName: Full=Thiogalactoside acetyltransferase;
GN   Name=lacA; OrderedLocusNames=LL1981; ORFNames=L0026;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 7962;
RA   Griffin H.G., Gasson M.J.;
RT   "The gene (lacA) encoding galactoside acetyltransferase from Lactococcus
RT   lactis.";
RL   Biotechnol. Lett. 16:1125-1130(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 7962;
RA   Lee J.M., Chung D.K., Park J.H., Lee W.K., Chang H.C., Kim J.H., Lee H.J.;
RT   "The organization of genes involved in metabolism of gal/lac of Lactococcus
RT   lactis.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-galactoside + acetyl-CoA = a 6-acetyl-beta-D-
CC         galactoside + CoA; Xref=Rhea:RHEA:15713, ChEBI:CHEBI:28034,
CC         ChEBI:CHEBI:28250, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.18;
CC         Evidence={ECO:0000250|UniProtKB:P07464};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P07464}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK06079.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X81358; CAA57126.1; -; Genomic_DNA.
DR   EMBL; U60828; AAD11503.1; -; Genomic_DNA.
DR   EMBL; AE005176; AAK06079.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; P52984; -.
DR   SMR; P52984; -.
DR   STRING; 272623.L0026; -.
DR   PaxDb; P52984; -.
DR   EnsemblBacteria; AAK06079; AAK06079; L0026.
DR   KEGG; lla:L0026; -.
DR   eggNOG; COG0110; Bacteria.
DR   HOGENOM; CLU_051638_7_5_9; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008870; F:galactoside O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005989; P:lactose biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR039369; LacA-like.
DR   InterPro; IPR024688; Mac_dom.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR43017; PTHR43017; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF12464; Mac; 1.
DR   SMART; SM01266; Mac; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Lactose biosynthesis; Reference proteome;
KW   Repeat; Transferase.
FT   CHAIN           1..207
FT                   /note="Galactoside O-acetyltransferase"
FT                   /id="PRO_0000068697"
FT   ACT_SITE        117
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P07464"
FT   BINDING         87
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P07464"
FT   BINDING         144
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P07464"
FT   BINDING         162
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P07464"
FT   BINDING         167..168
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P07464"
FT   BINDING         185
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P07464"
FT   SITE            87
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P07464"
FT   CONFLICT        83
FT                   /note="G -> E (in Ref. 3; AAK06079)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   207 AA;  23432 MW;  A7657F285F17066E CRC64;
     MPKLESYKRV HTEELYFPND QKLWKEQQEA LVLLEKFNQT SVTQPEQQME LLKKMFSEIG
     ENCFIQPPFY ANFGGKNVHF GTGIYANFNL TLVDDTDIFV GNHVMFGPNV TIDTATHPVS
     PDLRKRGAQY NKKVYIEENV WLGAGVIVLP GVRIGKNSVI GAGSLVTKDI PDNVVAFGTP
     CMVKRKINDS DFKTYDHGKK IDLDEFI