ID   HP2_ELSFA               Reviewed;         385 AA.
AC   B1A0U6;
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 HP2 {ECO:0000303|PubMed:18957608};
DE   Flags: Precursor;
GN   Name=HP2 {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}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is up-regulated during nitrogen starvation or at
CC       alkaline pH, conditions highly conducive to elsinochrome accumulation.
CC       {ECO:0000269|PubMed:18957608}.
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DR   EMBL; EU414200; ABZ82010.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1A0U6; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..385
FT                   /note="Elsinochromes biosynthesis cluster protein HP2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5002759954"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   385 AA;  43712 MW;  63ADE6239D8F98C3 CRC64;
     MVLLYILIMV ALIPMYMTVV QDATFSHPPP GLLIPEAWSG SGSIRLWTDA QEIPVRCFWK
     LVYDPRIHPE TAAIQQGDSI MYMYSGTRFL DYRTVLSALL LTFVFFWRML SMFDRSRNRF
     QRACVSIPSA LLEVCRQKAI KKTATLPFYG QALYFGIMCL YTAHIVLWDF LNSFAGTLWL
     ITLNLANGTA QIINLRKERH RNRHDEESSW TFGQIVPIVL LVSPLVAAFE DLLSKRSRRA
     LREGSVGNTS LNEVDLTPEP SLTEATTLSL HTRPLIYSVP TSITQSSIAS QKSSGTPAQD
     LIRSSWPYAI LFWELHVLLA FMVIWLPLAQ SQLFIFRYAY WEAYYAFPAA VGTFWLTVVI
     AVPFSSIGRS SYPCPKPRRS GLNVA