ID   ACUC_STAAS              Reviewed;         389 AA.
AC   Q6G8J2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Acetoin utilization protein AcuC;
GN   Name=acuC; OrderedLocusNames=SAS1661;
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   -!- FUNCTION: Role in growth on acetoin or butanediol. Involved in the
CC       breakdown of these compounds used as a carbon source (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Ketone degradation; acetoin degradation.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. {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; BX571857; CAG43464.1; -; Genomic_DNA.
DR   RefSeq; WP_001184010.1; NC_002953.3.
DR   AlphaFoldDB; Q6G8J2; -.
DR   SMR; Q6G8J2; -.
DR   KEGG; sas:SAS1661; -.
DR   HOGENOM; CLU_007727_8_0_9; -.
DR   OMA; GWLRAFH; -.
DR   UniPathway; UPA00040; -.
DR   GO; GO:0045150; P:acetoin catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd09994; HDAC_AcuC_like; 1.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR003085; AcuC.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01272; ACUCPROTEIN.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; SSF52768; 1.
PE   3: Inferred from homology;
KW   Acetoin catabolism.
FT   CHAIN           1..389
FT                   /note="Acetoin utilization protein AcuC"
FT                   /id="PRO_0000114734"
SQ   SEQUENCE   389 AA;  44659 MW;  7A5DB7C69AF4F4F3 CRC64;
     MQQHSSKTAY VYSDKLLQYR FHDQHPFNQM RLKLTTELLL NANLLSPEQI VQPRIATDDE
     LMLIHKYDYV EAIKHASHGI ISEDEAKKYG LNDEENSQFK HMHRHSATIV GGALTLADLI
     MSGKVLNGCH LGGGLHHAQP GRASGFCIYN DIAITAQYLA KEYNQRVLII DTDAHHGDGT
     QWSFYADNHV TTYSIHETGK FLFPGSGHYT ERGEDIGYGH TVNVPLEPYT EDASFLECFK
     LTVEPVVKSF KPDIILSVNG VDIHYRDPLT HLNCTLHSLY EIPYFVKYLA DSYTNGKVIM
     FGGGGYNIWR VVPRAWSHVF LSLIDQPIQS GYLPLEWINK WKHYSSELLP KRWEDRLNDY
     TYVPRTKEIS EKNKKLALHI ASWYESTRQ