ID   THLA_STAAB              Reviewed;         393 AA.
AC   Q2YVF5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Probable acetyl-CoA acyltransferase;
DE            EC=2.3.1.9;
DE   AltName: Full=Acetoacetyl-CoA thiolase;
GN   OrderedLocusNames=SAB0304;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC         ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10020};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ938182; CAI79992.1; -; Genomic_DNA.
DR   RefSeq; WP_000199088.1; NC_007622.1.
DR   AlphaFoldDB; Q2YVF5; -.
DR   SMR; Q2YVF5; -.
DR   KEGG; sab:SAB0304; -.
DR   HOGENOM; CLU_031026_0_0_9; -.
DR   OMA; ICPSIAI; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020610; Thiolase_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..393
FT                   /note="Probable acetyl-CoA acyltransferase"
FT                   /id="PRO_0000270502"
FT   ACT_SITE        88
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        349
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        378
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   393 AA;  41589 MW;  C331F8215FEA47E7 CRC64;
     MTRVVLAAAY RTPIGVFGGA FKDVPAYDLG ATLIEHIIKE TGLNPSEINE VIIGNVLQAG
     QGQNPARIAA MKGGLPETVP VFTVNKVCGS GLKSIQLAYQ SIVTGENDIV LAGGMENMSQ
     SPMLVNNSRF GFKMGHQSMV DSMVYDGLTD VFNQYHMGIT AENLVEQYGI SREEQDTFAV
     NSQKKAANAQ QNGGFDSEIV PVSIPQRKGE PIVVTKDEGV RENVSVEKLS RLRPAFKKDG
     TVTAGNASGI NDGAAMMLVM SEDKAKELNI EPLAVLDGFG SHGVDPSIMG IAPVGAVEKA
     LKRSKKELSD IDVFELNEAF AAQSLAVDRE LKLPPEKVNV KGGAIALGHP IGASGARVLV
     TLLHQLNDEV ETGLTSLCIG GGQAIAAVVS KYK