ID   VRAB_STAA1              Reviewed;         379 AA.
AC   Q9KWK4; A7WZ15;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Putative acetyl-CoA C-acetyltransferase VraB;
DE            EC=2.3.1.-;
GN   Name=vraB; OrderedLocusNames=SAHV_0574;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VANCOMYCIN RESISTANCE.
RX   PubMed=10708580; DOI=10.1006/bbrc.2000.2277;
RA   Kuroda M., Kuwahara-Arai K., Hiramatsu K.;
RT   "Identification of the up- and down-regulated genes in vancomycin-resistant
RT   Staphylococcus aureus strains Mu3 and Mu50 by cDNA differential
RT   hybridization method.";
RL   Biochem. Biophys. Res. Commun. 269:485-490(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
CC   -!- MISCELLANEOUS: May contribute to vancomycin resistance.
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; AB035449; BAB03328.1; -; Genomic_DNA.
DR   EMBL; AP009324; BAF77457.1; -; Genomic_DNA.
DR   PIR; B89826; B89826.
DR   RefSeq; WP_001070676.1; NC_009782.1.
DR   AlphaFoldDB; Q9KWK4; -.
DR   SMR; Q9KWK4; -.
DR   KEGG; saw:SAHV_0574; -.
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_0000206425"
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;  41094 MW;  B62F36E0A437A771 CRC64;
     MNQAVIVAAK RTAFGKYGGT LKHLEPEQLL KPLFQHFKEK YPEVISKIDD 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