ID   ACLF_ASPOR              Reviewed;         256 AA.
AC   Q2UPB8;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Aspirochlorine biosynthesis protein F {ECO:0000303|PubMed:25302411};
GN   Name=aclF {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000034;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=25302411; DOI=10.1002/anie.201407624;
RA   Chankhamjon P., Boettger-Schmidt D., Scherlach K., Urbansky B., Lackner G.,
RA   Kalb D., Dahse H.M., Hoffmeister D., Hertweck C.;
RT   "Biosynthesis of the halogenated mycotoxin aspirochlorine in koji mold
RT   involves a cryptic amino acid conversion.";
RL   Angew. Chem. Int. Ed. 53:13409-13413(2014).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       aspirochlorine (or antibiotic A30641), an unusual halogenated spiro
CC       compound with distinctive antifungal properties due to selective
CC       inhibition of protein biosynthesis, and which is also active against
CC       bacteria, viruses, and murine tumor cells (PubMed:25302411). The non-
CC       ribosomal peptide synthetase (NRPS) aclP is responsible the formation
CC       of the diketopiperazine (DKP) core from the condensation of 2
CC       phenylalanine residues (PubMed:25302411). One Phe residue is tailored
CC       into chlorotyrosine by hydroxylation and chlorination, whereas the
CC       second Phe undergoes an unprecedented C-C bond cleavage to be converted
CC       into glycine (PubMed:25302411). After formation of the DKP, sulfur is
CC       incorporated into the DKP by conjugation with glutathione by aclG,
CC       followed by its stepwise degradation to the thiol by aclI, aclJ and
CC       aclK, and the dithiol oxidation by aclT (PubMed:25302411). In addition,
CC       oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM
CC       and aclU) act as tailoring enzymes to produce the intermediate
CC       dechloroaspirochlorine (PubMed:25302411). Ultimately, chlorination of
CC       dechloroaspirochlorine by the halogenase aclH is the last step in the
CC       aspirochlorine pathway (PubMed:25302411).
CC       {ECO:0000269|PubMed:25302411}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25302411}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
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DR   EMBL; AP007154; BAE56597.1; -; Genomic_DNA.
DR   RefSeq; XP_001818599.2; XM_001818547.2.
DR   AlphaFoldDB; Q2UPB8; -.
DR   EnsemblFungi; BAE56597; BAE56597; AO090001000034.
DR   GeneID; 5990570; -.
DR   KEGG; aor:AO090001000034; -.
DR   HOGENOM; CLU_1157101_0_0_1; -.
DR   Proteomes; UP000006564; Chromosome 2.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..256
FT                   /note="Aspirochlorine biosynthesis protein F"
FT                   /id="PRO_0000441193"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   256 AA;  29015 MW;  8E3477DBA46AD8A9 CRC64;
     MSSTAFTSSL SNWDLYPTNG SITPHLLLVG AQILFLSGPH FHGRRTLAAT TILSLAAIAQ
     YNRFTNNPGV ANLFALAWPH WLSAVEKIVF ASPEGPEADL WRVDRVPREA MSWPVFGWRK
     VKWAVTLLLN LRGIRWSFQV KNVPKMPERM TRGQFLRWRL GELVWVLLMT DLVSQMMLRF
     FFTDAAGALG NLDSKYITIR DARWGWSLLK ALTFGLGPYF FINMQYLVVS ILAVAMGISR
     PEVGSCPPRR SNRQPC