ID   CRTQ_STAAR              Reviewed;         375 AA.
AC   Q6GDN6;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=4,4'-diaponeurosporenoate glycosyltransferase;
DE            EC=2.4.1.-;
GN   Name=crtQ; OrderedLocusNames=SAR2645;
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 glycosylation of 4,4'-diaponeurosporenoate,
CC       i.e. the esterification of glucose at the C1'' position with the
CC       carboxyl group of 4,4'-diaponeurosporenic acid, to form glycosyl-4,4'-
CC       diaponeurosporenoate. This is a step in the biosynthesis of
CC       staphyloxanthin, an orange pigment present in most staphylococci
CC       strains (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC       staphyloxanthin from farnesyl diphosphate: step 4/5.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. CrtQ
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BX571856; CAG41622.1; -; Genomic_DNA.
DR   RefSeq; WP_000871726.1; NC_002952.2.
DR   AlphaFoldDB; Q6GDN6; -.
DR   SMR; Q6GDN6; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   KEGG; sar:SAR2645; -.
DR   HOGENOM; CLU_038143_1_0_9; -.
DR   OMA; GWLGKPH; -.
DR   OrthoDB; 724641at2; -.
DR   UniPathway; UPA00029; UER00559.
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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis; Cell membrane; Glycosyltransferase; Membrane;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..375
FT                   /note="4,4'-diaponeurosporenoate glycosyltransferase"
FT                   /id="PRO_0000284860"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   375 AA;  42332 MW;  A1FAD8978F61FD07 CRC64;
     MKWLSRILTV IVTMSMACGA LIFNRRHQLK AKTLNFNHKA LTIIIPARNE EKRIGHLLHS
     IIQQQVPVDV IVMNDGSTDE TACVARSYGA TVVDVVDDAD GKWYGKSHAC YQGVTHACTN
     RIAFVDADVT FLRKDAVEAL INQYQLQGEK GLLSVQPYHI TKRFYEGFSA IFNLMTVVGM
     NVFSTLDDGR TNQHAFGPVT LTNKEDYYAT GGHKSANRHI IEGFALGSAY TSQSLPVTVY
     EGFPFVAFRM YQEGFQSLQE GWTKHLSTGA GGTKPKIMAA IVLWLFGSIA SILGLCLSLK
     YRQMSVGKML TVYLSYTTQF IYLHRRVGQF SNLLMVCHPL LFMFFTKIFI QSWKQTHRYG
     VVEWKGRQYS ISKEQ