ID   CRTO_STAAS              Reviewed;         165 AA.
AC   Q6G6A9;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Glycosyl-4,4'-diaponeurosporenoate acyltransferase;
DE            EC=2.3.1.-;
DE   Flags: Precursor;
GN   Name=crtO; OrderedLocusNames=SAS2451;
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: Catalyzes the acylation of glycosyl-4,4'-
CC       diaponeurosporenoate, i.e. the esterification of glucose at the C6''
CC       position with the carboxyl group of the C(15) fatty acid 12-
CC       methyltetradecanoic acid, to yield staphyloxanthin. This is the last
CC       step in the biosynthesis of this orange pigment, present in most
CC       staphylococci strains (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC       staphyloxanthin from farnesyl diphosphate: step 5/5.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acyltransferase CrtO family. {ECO:0000305}.
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DR   EMBL; BX571857; CAG44267.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6G6A9; -.
DR   KEGG; sas:SAS2451; -.
DR   HOGENOM; CLU_133300_0_0_9; -.
DR   OMA; FNLPCLW; -.
DR   UniPathway; UPA00029; UER00560.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR044021; CrtO.
DR   Pfam; PF18927; CrtO; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Carotenoid biosynthesis; Cell membrane; Membrane; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..165
FT                   /note="Glycosyl-4,4'-diaponeurosporenoate acyltransferase"
FT                   /id="PRO_0000284850"
FT   TRANSMEM        126..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   165 AA;  20319 MW;  A73479B1786566FA CRC64;
     MKTMKKYIKT AFFCSMYWLI VQLNIANLGT RIPDKYFRQK YIIFKSFNFE KHGKFWNKWF
     YVRKWKHKIL DGHQLNQNIY DQRHLMTINT DEIEKMIIET KRAELIHWIS ILPVIIFNKG
     PRLVKYINIF YAMIANVPII IVQRYNRPRL TQLLRILKRR GERHD