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CRTO_STAAB
ID   CRTO_STAAB              Reviewed;         165 AA.
AC   Q2YWE4;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Glycosyl-4,4'-diaponeurosporenoate acyltransferase;
DE            EC=2.3.1.-;
DE   Flags: Precursor;
GN   Name=crtO; OrderedLocusNames=SAB2438c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI82126.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2YWE4; -.
DR   KEGG; sab:SAB2438c; -.
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_0000284847"
FT   TRANSMEM        126..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   165 AA;  20307 MW;  045760379D0D4227 CRC64;
     MKTMKKYIKT AFFCSMYWLI VQLNIANLGT RIPDKYFRQK HIIFKSFNFE KHGKFWNKWF
     YVRKWKHKIL DGHQLNRNIY DQRHLMTINS DEIEKMIIET KRAELIHWIS ILPVIIFNKG
     PRLVKYINIF YAMIANVPII IVQRYNRPRL TQLLRILKRR GERHD
 
 
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