ID   PLE2_RHOPP              Reviewed;         377 AA.
AC   A0A6S6QLX9;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   23-FEB-2022, entry version 5.
DE   RecName: Full=Acetyltransferase ple2 {ECO:0000303|PubMed:28924980};
DE            EC=2.3.1.- {ECO:0000269|PubMed:28924980};
DE   AltName: Full=Pleuromutilin biosynthesis cluster protein 2 {ECO:0000303|PubMed:28924980};
DE   Flags: Precursor;
GN   Name=ple2 {ECO:0000303|PubMed:28924980};
OS   Rhodocybe pseudopiperita (Clitopilus pseudopiperitus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Entolomataceae; Rhodocybe.
OX   NCBI_TaxID=693819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=ATCC 20527;
RX   PubMed=28924980; DOI=10.1002/cbic.201700434;
RA   Yamane M., Minami A., Liu C., Ozaki T., Takeuchi I., Tsukagoshi T.,
RA   Tokiwano T., Gomi K., Oikawa H.;
RT   "Biosynthetic machinery of diterpene pleuromutilin isolated from
RT   basidiomycete fungi.";
RL   ChemBioChem 18:2317-2322(2017).
CC   -!- FUNCTION: Acetyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of pleuromutilin, a tricyclic diterpene showing
CC       antibacterial properties (PubMed:28924980). The geranylgeranyl
CC       diphosphate (GGPP) synthase ple4 catalyzes the first step in
CC       pleuromutilin biosynthesis (PubMed:28924980). GGPP is then substrate of
CC       the premutilin synthase (PS) ple3 to yield premutilin
CC       (PubMed:28924980). Premutilin synthase is a bifunctional enzyme
CC       composed of the fusion of a class II diterpene cyclase (DTC) and a
CC       class I diterpene synthase (DTS), with the corresponding domains and
CC       active sites containing characteristic aspartate-rich motifs (By
CC       similarity). GGPP is first converted to mutildienyl-diphosphate (MPP)
CC       at the class II DTC site (By similarity). MPP is subsequently further
CC       cyclized at the class I DTS site, followed by a 1,5-hydride shift and
CC       addition of water prior to terminating deprotonation, to yield
CC       premutilin (By similarity). The cytochrome P450 monooxygenases ple5 and
CC       ple6 hydroxylate premutilin at C-11 and C-3, respectively, producing
CC       11-hydroxypremutilin and 3-hydroxypremutilin (PubMed:28924980). The
CC       combination of the actions of both ple5 and ple6 leads to the
CC       production of 3,11-dihydroxypremutilin (PubMed:28924980). The short
CC       chain dehydrogenase ple7 further converts 3,11-dihydroxypremutilin into
CC       mutilin (PubMed:28924980). The acetyltransferase ple2 then acetylates
CC       mutilin to produce 14-O-acetylmutilin (PubMed:28924980). Finally, the
CC       cytochrome P450 monooxygenase ple1 catalyzes hydroxylation on the alpha
CC       position of the acetyl side chain of 14-O-acetylmutilin to yield
CC       pleuromutilin (PubMed:28924980). {ECO:0000250|UniProtKB:A0A2L0VXR0,
CC       ECO:0000269|PubMed:28924980}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:28924980}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the wax synthase family. {ECO:0000305}.
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DR   EMBL; LC314149; BCI98770.1; -; Genomic_DNA.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR044851; Wax_synthase.
DR   InterPro; IPR032805; Wax_synthase_dom.
DR   PANTHER; PTHR31595; PTHR31595; 1.
DR   Pfam; PF13813; MBOAT_2; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Membrane; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..377
FT                   /note="Acetyltransferase ple2"
FT                   /id="PRO_5028296751"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   377 AA;  43171 MW;  06AD422A1E07C484 CRC64;
     MKPFSPELLV LSFILLVLSC AIRPAKGRWI LWVIIVALNT YLTMTTTGDS TLDYDIANNL
     FVITLTATDY ILLTDVQREL QFRNQKGVEQ ASLLERIKWA TWLVQSRRGV GWNWEPKIFV
     HRFSPKTSRL SFLLQQLVTG ARHYLICDLV SLYSRSPVAF AEPLASRPLI WRCADIAAWL
     LFTTNQVSIL LTALSLMQVL SGYSEPQDWV PVFGRWRDAY TVRRFWGRSW HQLVRRCLSS
     PGKYLSTKVL GLKPGSNPAL YVQLYAAFFL SGVLHAIGDF KVHEDWYKAG TMEFFCVQAV
     IIQMEDGVLW VGRKLGIKET WYWRALGHLW TVAWFVYSCP NWLGATISGR GKASMALESS
     LVLGLYRGEW HPPRVAQ