ID   VRAB_STAAR              Reviewed;         379 AA.
AC   Q6GJ93;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Putative acetyl-CoA C-acetyltransferase VraB;
DE            EC=2.3.1.-;
GN   Name=vraB; OrderedLocusNames=SAR0581;
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   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; BX571856; CAG39601.1; -; Genomic_DNA.
DR   RefSeq; WP_001070682.1; NC_002952.2.
DR   AlphaFoldDB; Q6GJ93; -.
DR   SMR; Q6GJ93; -.
DR   KEGG; sar:SAR0581; -.
DR   HOGENOM; CLU_031026_2_1_9; -.
DR   OMA; GHPWGAS; -.
DR   OrthoDB; 1058688at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
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; PS00737; THIOLASE_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..379
FT                   /note="Putative acetyl-CoA C-acetyltransferase VraB"
FT                   /id="PRO_0000206429"
FT   ACT_SITE        86
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        338
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  40974 MW;  2E260D8FB395AF9D CRC64;
     MNQAVIVAAK RTAFGKYGGT LKHLEPEQLL KPLFQHFKEK YPEVISKIDD VVLGNVVGNG
     GNIARKALLE AGLKDSIPGV TIDRQCGSGL ESVQYACRMI QAGAGKVYIA GGVESTSRAP
     WKIKRPHSVY ETALPEFYER ASFAPEMSDP SMIQGAENVA KMYGVSRELQ DEFAYRSHQL
     TAENVKNGNI SQEILPITVK GELFNTDESL KSHIPKDNFG RFKPVIKGGT VTAANSCMKN
     DGAVLLLIME KDMAYELGFD HGLLFKDGVT VGVDSNLPGI GPVPAISNLL KRNQLTIENI
     EVIEINEAFS AQVVACQQAL NISNTQLNIW GGALASGHPY GASGAQLVTR LFYMFDKESM
     IASMGIGGGL GNAALFTRF