ID   THLA_STAAR              Reviewed;         393 AA.
AC   Q6GJW4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Probable acetyl-CoA acyltransferase;
DE            EC=2.3.1.9;
DE   AltName: Full=Acetoacetyl-CoA thiolase;
GN   OrderedLocusNames=SAR0351;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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}.
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; BX571856; CAG39374.1; -; Genomic_DNA.
DR   RefSeq; WP_000199080.1; NC_002952.2.
DR   AlphaFoldDB; Q6GJW4; -.
DR   SMR; Q6GJW4; -.
DR   KEGG; sar:SAR0351; -.
DR   HOGENOM; CLU_031026_0_0_9; -.
DR   OMA; ICPSIAI; -.
DR   OrthoDB; 1058688at2; -.
DR   Proteomes; UP000000596; Chromosome.
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_0000270506"
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;  41745 MW;  83F128026C6EFB86 CRC64;
     MTRVVLAAAY RTPIGVFGGA FKDVPAYDLG ATLIEHIIKE TGLNPSEINE VIIGNVLQAG
     QGQNPARIAA MKGGLPETVP AFTVNKVCGS GLKSIQLAYQ SIVTGENDIV LAGGMENMSQ
     SPMLVNNSRF GFKMGHQSMV DSMVYDGLTD VFNQYHMGIT AENLVEQYGI SREEQDTFAV
     NSQQKAVRAQ QNGEFDSEIV PVSIPQRKGE PIVVTKDEGV RENVSVEKLS RLRPAFKKDG
     TVTAGNASGI NDGAAMMLVM SEDKAKELNI EPLAVLDGFG SHGVDPAIMG IAPVDAVEKA
     LKRSKKELSD IDVFELNEAF AAQSLAVDRE LKLPPEKVNV KGGAIALGHP IGASGARVLV
     TLLHQLNDEV ETGLTSLCIG GGQAIAAVVS KYK