FRBF_BLOB1
ID FRBF_BLOB1 Reviewed; 361 AA.
AC A0A0S6XAX9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=C2H2-type zinc-finger transcription factor frbF {ECO:0000303|PubMed:27660098};
DE AltName: Full=FR901469 biosynthesis cluster protein F {ECO:0000303|PubMed:27660098};
GN Name=frbF {ECO:0000303|PubMed:27660098}; ORFNames=ANO11243_029900;
OS Fungal sp. (strain No.11243).
OC Eukaryota; Fungi.
OX NCBI_TaxID=1603295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25838475; DOI=10.1128/genomea.00118-15;
RA Matsui M., Yokoyama T., Nemoto K., Kumagai T., Terai G., Arita M.,
RA Machida M., Shibata T.;
RT "Genome sequence of fungal species No.11243, which produces the antifungal
RT antibiotic FR901469.";
RL Genome Announc. 3:0-0(2015).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=11099224; DOI=10.7164/antibiotics.53.912;
RA Fujie A., Iwamoto T., Muramatsu H., Okudaira T., Nitta K., Nakanishi T.,
RA Sakamoto K., Hori Y., Hino M., Hashimoto S., Okuhara M.;
RT "FR901469, a novel antifungal antibiotic from an unidentified fungus
RT No.11243. I. Taxonomy, fermentation, isolation, physico-chemical properties
RT and biological properties.";
RL J. Antibiot. 53:912-919(2000).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=11099225; DOI=10.7164/antibiotics.53.920;
RA Fujie A., Iwamoto T., Muramatsu H., Okudaira T., Sato I., Furuta T.,
RA Tsurumi Y., Hori Y., Hino M., Hashimoto S., Okuhara M.;
RT "FR901469, a novel antifungal antibiotic from an unidentified fungus
RT No.11243. II. In vitro and in vivo activities.";
RL J. Antibiot. 53:920-927(2000).
RN [4]
RP FUNCTION.
RX PubMed=27660098; DOI=10.1016/j.jbiosc.2016.08.007;
RA Matsui M., Yokoyama T., Nemoto K., Kumagai T., Terai G., Tamano K.,
RA Machida M., Shibata T.;
RT "Identification of a putative FR901469 biosynthesis gene cluster in fungal
RT sp. No. 11243 and enhancement of the productivity by overexpressing the
RT transcription factor gene frbF.";
RL J. Biosci. Bioeng. 123:147-153(2017).
RN [5]
RP FUNCTION.
RX PubMed=28341398; DOI=10.1016/j.jbiosc.2017.02.015;
RA Matsui M., Yokoyama T., Nemoto K., Kumagai T., Tamano K., Machida M.,
RA Shibata T.;
RT "Further enhancement of FR901469 productivity by co-overexpression of cpcA,
RT a cross-pathway control gene, and frbF in fungal sp. No. 11243.";
RL J. Biosci. Bioeng. 124:8-14(2017).
CC -!- FUNCTION: C2H2-type zinc-finger transcription factor; part of the gene
CC cluster that mediates the biosynthesis of the antifungal antibiotic
CC FR901469, an inhibitor of beta-1,3-glucansynthase, exerting antifungal
CC activity against the pathogenes Candida albicans and Aspergillus
CC fumigatus (PubMed:27660098). FR901469 is a cyclic depsipeptide
CC containing 12 amino acid residues and a fatty acid chain
CC (PubMed:27660098). Positively regulates the expression of the FR901469
CC biosynthesis cluster genes frbA, frbB, frbC, frbG, frbH and frbI
CC (PubMed:27660098, PubMed:28341398). Affects also the expression of some
CC genes involved in other metabolic pathways, including the ergosterol
CC biosynthetic pathway, beta-1,3-glucan catabolic enzymes or chitinases
CC (PubMed:27660098). {ECO:0000269|PubMed:27660098,
CC ECO:0000269|PubMed:28341398}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:27660098}.
CC -!- BIOTECHNOLOGY: FR901469 inhibits the activity of 1,3-beta-glucan
CC synthase from Candida albicans and Aspergillus fumigatus
CC (PubMed:11099224, PubMed:11099225). With minimal inhibitory
CC concentrations (MICs) against Candida albicans and Aspergillus
CC fumigatus of 0.63 ug/ml and 0.16 ug/ml, repectively, FR901469 displays
CC greater inhibitory activity than other 1,3-beta-glucan synthase
CC inhibitors such as, WF11899A, echinocandin B, aculeacin A, and
CC papulacandin B (PubMed:11099224, PubMed:11099225).
CC {ECO:0000269|PubMed:11099224, ECO:0000269|PubMed:11099225}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; DF938583; GAM84987.1; -; Genomic_DNA.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000054361; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Translation regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..361
FT /note="C2H2-type zinc-finger transcription factor frbF"
FT /id="PRO_0000454575"
FT ZN_FING 325..345
FT /note="C2H2-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 70..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 39440 MW; 9DA22F33546C3D81 CRC64;
MHCPQSARKT RQQQQHPLTD RCAYAGSANM PSAVAIPAPL PPSNCEEGIW LSKSVLMSLL
FPNQALPAAH QVSSVETPST STTSTSTTTS TSRAASEFDA NYCNTVRNPY IPPTPEDKFP
VTPPPSLDQT AMSSPAACIP HESGPVRPKQ TVAFTPGFSN PYPAFIEQSS VSMPVYEPTP
HLHTQPQTQS RPSTQTPHQH QQQPYTFATP PYQPYDHIYS PELDLSLLST DFSLYPQHPQ
HPQIPPPDLS LWSPSIDAAS PLAASSPDPT TLWAPAIPIA PPQPASKQDG PIPRCWDHGC
NGRRFSSIGN LVRHIKEQNG PRARFECRRC GQTFTRSTAR SMHVKRGRCE GTMRSKGIGG
K
