ID   HP3_ELSFA               Reviewed;         249 AA.
AC   B1A0U7;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Elsinochromes biosynthesis cluster protein HP3 {ECO:0000303|PubMed:18957608};
GN   Name=HP3 {ECO:0000303|PubMed:18957608};
OS   Elsinoe fawcettii (Citrus scab fungus) (Sphaceloma fawcettii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX   NCBI_TaxID=40997;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND INDUCTION.
RX   PubMed=18957608; DOI=10.1099/mic.0.2008/019414-0;
RA   Chung K.R., Liao H.L.;
RT   "Determination of a transcriptional regulator-like gene involved in
RT   biosynthesis of elsinochrome phytotoxin by the citrus scab fungus, Elsinoe
RT   fawcettii.";
RL   Microbiology 154:3556-3566(2008).
RN   [2]
RP   REVIEW.
RX   PubMed=21199563; DOI=10.1111/j.1364-3703.2010.00663.x;
RA   Chung K.R.;
RT   "Elsinoe fawcettii and Elsinoe australis: the fungal pathogens causing
RT   citrus scab.";
RL   Mol. Plant Pathol. 12:123-135(2011).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       elsinochromes, pigments consisting of at least four interconvertible
CC       tautomers (A, B, C and D) that have a core phenolic quinone to which
CC       various side chains are attached and which play an important role in
CC       fungal pathogenesis (PubMed:18957608). The non-reducing polyketide
CC       synthase PKS1 was proposed to iteratively catalyze decarboxylation
CC       between acetyl-CoA and malonyl-CoA subunits for polyketide chain
CC       elongation. The released polyketide undergoes cyclization to form an
CC       aromatic ring, and proceeds via serial modification steps to produce
CC       the heptaketide back- bone of elsinochrome. As elsinochrome has a
CC       symmetrical structure, two identical heptaketides are fused to form a
CC       core 1,2-dihydrobenzo-perylene ring structure, which can then be
CC       successively modified to produce the various derivatives of
CC       elsinochrome. Some of these reactions may be cooperatively carried out,
CC       at least in part, by the products of RDT1, OXR1 and PKS1. PRF1,
CC       embedded within the elsinochrome cluster possibly functions to
CC       stabilize some of the biosynthetic enzymes required for elsinochrome
CC       production. As prefoldin is a hexamer containing 2 a and 4 b subunits,
CC       additional prefoldin subunits, whose coding genes may not immediately
CC       link to the elsinochrome biosynthetic gene cluster, are required to
CC       fulfill the chaperone function. In addition, no methyltransferase-
CC       coding gene exists within the biosynthetic gene cluster, even though
CC       elsinochrome has four methyl groups at positions C3, C7, C8 and C12.
CC       Apparently, the identified gene cluster does not contain the entire
CC       entourage of genes responsible for elsinochrome biosynthesis. Once
CC       elsinochrome is synthesized, it must be exported outside the fungal
CC       cells, which is probably accomplished by the ECT1 transporter, to avoid
CC       toxicity (PubMed:21199563). {ECO:0000269|PubMed:18957608,
CC       ECO:0000303|PubMed:21199563}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is not affected in the presence of large amounts
CC       of glucose, during nitrogen starvation or at alkaline pH, conditions
CC       highly conducive to elsinochrome accumulation.
CC       {ECO:0000269|PubMed:18957608}.
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DR   EMBL; EU414201; ABZ82011.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1A0U7; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..249
FT                   /note="Elsinochromes biosynthesis cluster protein HP3"
FT                   /id="PRO_0000445825"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   249 AA;  27713 MW;  6282A0206FC8C6CC CRC64;
     MSDSASPIFV EYRNTDLLLS PSSAHVYYLP VSSDKHIMLT ASTTMGAVPL TTSTTPLVSS
     TVHQTVFRLR FDSAVTRLTP VTTTTSVTTG TLPWYIYQTP LVEIINTTRV TIGAPYDCDG
     FFWGRELRPN PDISGVGVVF AFMLSAWLVW LITVYAFARG QIDASQVTSA DTRFFRVQVK
     SSGWRWSSVF LRAILVFSDQ QLVTGIAIMI ATFASCQDIS VWHYAFAVSL AWVSHQHYCS
     LKTQHCVLD