ID   CRTO_STAAR              Reviewed;         165 AA.
AC   Q6GDN4;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Glycosyl-4,4'-diaponeurosporenoate acyltransferase;
DE            EC=2.3.1.-;
DE   Flags: Precursor;
GN   Name=crtO; OrderedLocusNames=SAR2647;
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   -!- 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}.
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; BX571856; CAG41624.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6GDN4; -.
DR   PRIDE; Q6GDN4; -.
DR   KEGG; sar:SAR2647; -.
DR   HOGENOM; CLU_133300_0_0_9; -.
DR   OMA; FNLPCLW; -.
DR   UniPathway; UPA00029; UER00560.
DR   Proteomes; UP000000596; Chromosome.
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_0000284849"
FT   TRANSMEM        126..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   165 AA;  20331 MW;  9116BED10C91F183 CRC64;
     MKIMKKYIKT AFFCSMYWLI VQLNIANLGT RIPDKYFRQK HIIFKSFNFE KHGKFWNKWF
     YVRKWKHKIL DGHKLNRNIY DQRHLMTINI DEIEKMIIET KRAELIHWIS ILPVIIFNKG
     PRVVKYINIF YAMIANVPII IVQRYNRPRL TQLLRILKRR GERHD