USTA_ASPFN
ID USTA_ASPFN Reviewed; 237 AA.
AC B8NM66;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Ribosomally synthesized cyclic peptide ustiloxin B precursosr {ECO:0000303|PubMed:24841822};
DE AltName: Full=Ustiloxin B biosynthesis protein A {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-I {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-II {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-III {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-IV {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-V {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-VI {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-VII {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-VIII {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-IX {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-X {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-XI {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-XII {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-XIII {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-XIV {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-XV {ECO:0000303|PubMed:24841822};
DE Contains:
DE RecName: Full=YAIG-XVI {ECO:0000303|PubMed:24841822};
DE Flags: Precursor;
GN Name=ustA {ECO:0000303|PubMed:24841822}; ORFNames=AFLA_094980;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, CLEAVAGE BY KEX2, AND POST-TRANSLATIONAL
RP MODIFICATIONS TO YIELD USTILOXIN B.
RX PubMed=24841822; DOI=10.1016/j.fgb.2014.04.011;
RA Umemura M., Nagano N., Koike H., Kawano J., Ishii T., Miyamura Y.,
RA Kikuchi M., Tamano K., Yu J., Shin-ya K., Machida M.;
RT "Characterization of the biosynthetic gene cluster for the ribosomally
RT synthesized cyclic peptide ustiloxin B in Aspergillus flavus.";
RL Fungal Genet. Biol. 68:23-30(2014).
RN [3]
RP FUNCTION, AND POST-TRANSLATIONAL MODIFICATIONS TO YIELD USTILOXIN B.
RX PubMed=27166860; DOI=10.1002/anie.201602611;
RA Ye Y., Minami A., Igarashi Y., Izumikawa M., Umemura M., Nagano N.,
RA Machida M., Kawahara T., Shin-Ya K., Gomi K., Oikawa H.;
RT "Unveiling the biosynthetic pathway of the ribosomally synthesized and
RT post-translationally modified peptide ustiloxin B in filamentous fungi.";
RL Angew. Chem. Int. Ed. 55:8072-8075(2016).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND POST-TRANSLATIONAL MODIFICATIONS TO
RP YIELD USTILOXIN B.
RX PubMed=26703898; DOI=10.1016/j.fgb.2015.12.010;
RA Nagano N., Umemura M., Izumikawa M., Kawano J., Ishii T., Kikuchi M.,
RA Tomii K., Kumagai T., Yoshimi A., Machida M., Abe K., Shin-ya K., Asai K.;
RT "Class of cyclic ribosomal peptide synthetic genes in filamentous fungi.";
RL Fungal Genet. Biol. 86:58-70(2016).
CC -!- FUNCTION: Ribosomally synthesized cyclic peptide ustiloxin B precursor:
CC Part of the gene cluster that mediates the biosynthesis of the
CC secondary metabolite ustiloxin B, an antimitotic tetrapeptide
CC (PubMed:24841822). The ustA translated product contains a 16-fold
CC repeated peptide embedding the tetrapeptide Tyr-Ala-Ile-Gly, that is
CC converted into the cyclic moiety of ustiloxin B (PubMed:24841822).
CC {ECO:0000269|PubMed:24841822}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:24841822}.
CC -!- PTM: UstA is processed by the subtilisin-like endoprotease kex2 that is
CC outside the ustiloxin B gene cluster, at the C-terminal side of Arg-
CC Lys, after transfer to Golgi apparatus through the endoplasmic
CC reticulum (ER) (PubMed:24841822). Cleavage by kex2 generates 16
CC peptides YAIG-I to YAIG-XVI (PubMed:24841822). To process the precursor
CC peptide further, at least two peptidases are necessary to cleave the N-
CC terminal and C-terminal sides of the Tyr-Ala-Ile-Gly core peptide which
CC serves as backbone for the synthesis of ustiloxin B, through
CC cyclization and modification of the tyrosine (PubMed:24841822). One of
CC the two peptidases must be the serine peptidase ustP; and the other
CC pepdidase is probably ustH (PubMed:24841822). Macrocyclization of the
CC core peptide derived from ustA requires the tyrosinase ustQ, as well as
CC the homologous oxidases ustYa and ustYb, and leads to the production of
CC the first cyclization product N-desmethylustiloxin F (PubMed:27166860,
CC PubMed:26703898). For the formation of N-desmethylustiloxin F, three
CC oxidation steps are required, hydroxylation at the benzylic position,
CC hydroxylation at either the aromatic ring of Tyr or beta-position of
CC Ile, and oxidative cyclization (PubMed:27166860). UstQ may catalyze the
CC oxidation of a phenol moiety, whereas the ustYa and ustYb are most
CC likely responsible for the remaining two-step oxidations
CC (PubMed:27166860). N-desmethylustiloxin F is then methylated by ustM to
CC yield ustiloxin F which in turn substrate of the cytochrome P450
CC monooxygenase ustC which catalyzes the formation of S-deoxyustiloxin H
CC (PubMed:27166860). The flavoprotein monooxygenases ustF1 and ustF2 then
CC participate in the modification of the side chain of S-deoxyustiloxin
CC H, leading to the synthesis of an oxime intermediate, via ustiloxin H
CC (PubMed:27166860). Finally, carboxylative dehydration performed by the
CC cysteine desulfurase-like protein ustD yields ustiloxin B
CC (PubMed:27166860). {ECO:0000269|PubMed:24841822,
CC ECO:0000269|PubMed:26703898, ECO:0000269|PubMed:27166860}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of ustiloxin B and its
CC intermediate ustiloxin F (PubMed:24841822, PubMed:26703898).
CC {ECO:0000269|PubMed:24841822, ECO:0000269|PubMed:26703898}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ963480; EED49417.1; -; Genomic_DNA.
DR RefSeq; XP_002381318.1; XM_002381277.1.
DR AlphaFoldDB; B8NM66; -.
DR STRING; 332952.B8NM66; -.
DR EnsemblFungi; EED49417; EED49417; AFLA_094980.
DR VEuPathDB; FungiDB:AFLA_094980; -.
DR eggNOG; ENOG502SJ4U; Eukaryota.
DR HOGENOM; CLU_1384495_0_0_1; -.
DR OMA; VEDYAIG; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
PE 1: Evidence at protein level;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..22
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437276"
FT CHAIN 23..35
FT /note="YAIG-I"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_5002878297"
FT CHAIN 36..48
FT /note="YAIG-II"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437277"
FT CHAIN 49..61
FT /note="YAIG-III"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437278"
FT CHAIN 62..74
FT /note="YAIG-IV"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437279"
FT CHAIN 75..87
FT /note="YAIG-V"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437280"
FT CHAIN 88..100
FT /note="YAIG-VI"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437281"
FT CHAIN 101..113
FT /note="YAIG-VII"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437282"
FT CHAIN 114..126
FT /note="YAIG-VIII"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437283"
FT CHAIN 127..139
FT /note="YAIG-IX"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437284"
FT CHAIN 140..152
FT /note="YAIG-X"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437285"
FT CHAIN 153..166
FT /note="YAIG-XI"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437286"
FT CHAIN 167..179
FT /note="YAIG-XII"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437287"
FT CHAIN 180..192
FT /note="YAIG-XIII"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437288"
FT CHAIN 193..206
FT /note="YAIG-XIV"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437289"
FT CHAIN 207..219
FT /note="YAIG-XV"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437290"
FT CHAIN 220..233
FT /note="YAIG-XVI"
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437291"
FT PROPEP 234..237
FT /evidence="ECO:0000305|PubMed:24841822"
FT /id="PRO_0000437292"
SQ SEQUENCE 237 AA; 26055 MW; 0B73041EFE0EF39D CRC64;
MKLILTLLVS GLCALAAPAA KRDGVEDYAI GIDKRNSVED YAIGIDKRNS VEDYAIGIDK
RNSVEDYAIG IDKRNSVEDY AIGIDKRNTV EDYAIGIDKR NSVEDYAIGI DKRNTVEDYA
IGIDKRNSVE DYAIGIDKRN SVEDYAIGID KRGGSVEDYA IGIDKRNSVE DYAIGIDKRN
SVEDYAIGID KRGSVEDYAI GIDKKRGTVE DYAIGIDKRG GSVEDYAIGI DKRHGGH
