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CRTQ_STAAS
ID   CRTQ_STAAS              Reviewed;         375 AA.
AC   Q6G6B1;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=4,4'-diaponeurosporenoate glycosyltransferase;
DE            EC=2.4.1.-;
GN   Name=crtQ; OrderedLocusNames=SAS2449;
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 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; BX571857; CAG44265.1; -; Genomic_DNA.
DR   RefSeq; WP_000871731.1; NC_002953.3.
DR   AlphaFoldDB; Q6G6B1; -.
DR   SMR; Q6G6B1; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   KEGG; sas:SAS2449; -.
DR   HOGENOM; CLU_038143_1_0_9; -.
DR   OMA; GWLGKPH; -.
DR   UniPathway; UPA00029; UER00559.
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_0000284861"
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;  42544 MW;  B0C0C2B6A5F2600B CRC64;
     MKWLSRILTV IVTMSMACGA LIFNRRHQLK AKTLNFNHKA LTIIIPARNE EKRIGHLLHS
     IIQQQVPVDV IVMNDGSTDE TARVARSYGA TVVDVVDDTD GKWYGKSHAC YQGVTHACTN
     RIAFVDADVT FLRKDAVETL INQYQLQGEK GLLSVQPYHI TKRFYEGFSA IFNLMTVVGM
     NVFSTLDDGR TNQHAFGPVT LTNKEDYYAT GGHKSANRHI IEGFALGSAY TSQSLPVTVY
     EGFPFVAFRM YQEGFQSLQE GWTKHLSTGA GGTKPKIMTA IVLWLFGSIA SILGLCLSLK
     YRQMSVRKMV ALYLSYTTQF IYLHRRVGQF SNLLMVCHPL LFMFFTKIFI QSWKQTHRYG
     VVEWKGRQYS ISKEQ
 
 
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