ID   CRTO_STAAE              Reviewed;         165 AA.
AC   Q53588; A6QK55;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Glycosyl-4,4'-diaponeurosporenoate acyltransferase;
DE            EC=2.3.1.-;
DE   Flags: Precursor;
GN   Name=crtO; OrderedLocusNames=NWMN_2465;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX   PubMed=16020541; DOI=10.1074/jbc.m505070200;
RA   Pelz A., Wieland K.-P., Putzbach K., Hentschel P., Albert K., Goetz F.;
RT   "Structure and biosynthesis of staphyloxanthin from Staphylococcus
RT   aureus.";
RL   J. Biol. Chem. 280:32493-32498(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
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. {ECO:0000269|PubMed:16020541}.
CC   -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC       staphyloxanthin from farnesyl diphosphate: step 5/5.
CC       {ECO:0000269|PubMed:16020541}.
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; X97985; CAA66625.1; -; Genomic_DNA.
DR   EMBL; AP009351; BAF68737.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53588; -.
DR   EnsemblBacteria; BAF68737; BAF68737; NWMN_2465.
DR   KEGG; sae:NWMN_2465; -.
DR   HOGENOM; CLU_133300_0_0_9; -.
DR   OMA; FNLPCLW; -.
DR   BRENDA; 2.3.1.B26; 3352.
DR   UniPathway; UPA00029; UER00560.
DR   Proteomes; UP000006386; 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_0000284846"
FT   TRANSMEM        126..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        48
FT                   /note="N -> K (in Ref. 1; CAA66625)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   165 AA;  20291 MW;  A73479B1787256FA CRC64;
     MKTMKKYIKT AFFCSMYWLI VQLNIANLGT RIPDKYFRQK YIIFKSFNFE KHGKFWNKWF
     YVRKWKHKIL DGHQLNQNIY DQRHLMTINT DEIEKMIIET KRAELIHWIS ILPVIIFNKG
     PRLVKYINIF YAMIANVPII IVQRYNRPRL TQLLRILKRK GERHD