ID   HP1_ELSFA               Reviewed;         311 AA.
AC   B1A0U5;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Elsinochromes biosynthesis cluster protein HP1 {ECO:0000303|PubMed:18957608};
GN   Name=HP1 {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 positively regulated by the cluster-specific
CC       transcription factor TSF1 (PubMed:18957608). Expression is up-regulated
CC       during nitrogen starvation (PubMed:18957608).
CC       {ECO:0000269|PubMed:18957608}.
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DR   EMBL; EU414199; ABZ82009.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1A0U5; -.
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..311
FT                   /note="Elsinochromes biosynthesis cluster protein HP1"
FT                   /id="PRO_0000445824"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   311 AA;  34829 MW;  8213AC545F1F77C4 CRC64;
     MTTTLYRDYG RPEYTPSVQT FRRTNLQVTY NETWTQPTTL AVSTSTTTIT AGAFETRWVD
     VSIVESVNIV IGAAPNCDGY FIGGKNVEPN PDISGIGVLA AFLVSAWVVW ATVLYAFARG
     QADAEQVKAS DVRFFRARGG DRQRAGKFRR AILVLSDQQL VTGIAILAAA FANLDGISVY
     HYTFAVRLAW LSSSVHLSTL LLLRRYLREH RRYLWFRVGG MTLLFVMLMI SLLPTYMYAF
     QEINEDTTSY INLRPANGIP AGCFWRVLAS WRPPIDVVKA SYSPGYWYFR SGKVGVDGQS
     IISAFIPAFT F