ID   VRAB_STAAS              Reviewed;         379 AA.
AC   Q6GBR1;
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=SAS0534;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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; BX571857; CAG42309.1; -; Genomic_DNA.
DR   RefSeq; WP_001070666.1; NC_002953.3.
DR   AlphaFoldDB; Q6GBR1; -.
DR   SMR; Q6GBR1; -.
DR   KEGG; sas:SAS0534; -.
DR   HOGENOM; CLU_031026_2_1_9; -.
DR   OMA; GHPWGAS; -.
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_0000206430"
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;  41110 MW;  1EE23B78F53F7E39 CRC64;
     MNQAVIVAAK RTAFGKYGGT LKHLEPEQLL KPLFQHFKEK YLEVISKIDD VVLGNVVGNG
     GNIARKALLE AGLKDSIPGV TIDRQCGSGL ESVQYACRMI QAGAGKVYIA GGVESTSRAP
     WKIKRPHSVY ETALPEFYER ASFAPEMSDP SMIQGAENVA KMYDVSRELQ DEFAYRSHQL
     TAENVKNGNI SQEILPITVK GEIFNTDESL KSHIPKDNFG RFKPVIKGGT VTAANSCMKN
     DGAVLLLIME KDMAYELGFE HGLLFKDGVT VGVDSNFPGI GPVPAISNLL KRNQLTIENI
     EVIEINEAFS AQVVACQQAL NISNTQLNIW GGALASGHPY GASGAQLVTR LFYMFDKETM
     IASMGIGGGL GNAALFTRF