VRTR2_PENAE
ID VRTR2_PENAE Reviewed; 836 AA.
AC D7PHY7;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Transcription factor vrtR2 {ECO:0000303|PubMed:20534346};
DE AltName: Full=Viridicatumtoxin synthesis protein R2 {ECO:0000303|PubMed:20534346};
GN Name=vrtR2 {ECO:0000303|PubMed:20534346};
OS Penicillium aethiopicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36650;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=IBT 5753;
RX PubMed=20534346; DOI=10.1016/j.chembiol.2010.03.015;
RA Chooi Y.H., Cacho R., Tang Y.;
RT "Identification of the viridicatumtoxin and griseofulvin gene clusters from
RT Penicillium aethiopicum.";
RL Chem. Biol. 17:483-494(2010).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=19168978; DOI=10.1038/ja.2008.84;
RA Zheng C.J., Yu H.E., Kim E.H., Kim W.G.;
RT "Viridicatumtoxin B, a new anti-MRSA agent from Penicillium sp. FR11.";
RL J. Antibiot. 61:633-637(2008).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=27049441; DOI=10.1038/ja.2016.35;
RA Inokoshi J., Nakamura Y., Komada S., Komatsu K., Umeyama H., Tomoda H.;
RT "Inhibition of bacterial undecaprenyl pyrophosphate synthase by small
RT fungal molecules.";
RL J. Antibiot. 69:798-805(2016).
CC -!- FUNCTION: Probable transcription factor that regulates expression of
CC the gene cluster that mediates the biosynthesis of viridicatumtoxin, a
CC tetracycline-like fungal meroterpenoid with a unique, fused
CC spirobicyclic ring system (PubMed:20534346).
CC {ECO:0000269|PubMed:20534346}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- BIOTECHNOLOGY: Viridicatumtoxin and its derivative, viridicatumtoxin B,
CC exhibit anti-methicillin-resistant Staphylococcus aureus (anti-MRSA)
CC activity (PubMed:19168978). Moreover, viridicatumtoxin and a C2 acetyl
CC analog, spirohexaline, have been demonstrated to inhibit bacterial
CC undecaprenyl diphosphate synthase, a potential new target for
CC antibiotic development (PubMed:27049441). {ECO:0000269|PubMed:19168978,
CC ECO:0000269|PubMed:27049441}.
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DR EMBL; GU574477; ADI24939.1; -; Genomic_DNA.
DR AlphaFoldDB; D7PHY7; -.
DR SMR; D7PHY7; -.
DR PRIDE; D7PHY7; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..836
FT /note="Transcription factor vrtR2"
FT /id="PRO_0000436818"
FT DNA_BIND 37..63
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 92125 MW; 2BE8F95D5FA7F81B CRC64;
MPSLSSKTST MQRSCRPQMS ACPNQQQKDR PVPQLSCVLC RDRKLKCDKL DPCSNCTSSG
VACTPIYRPR LPRGRHARTV QTKASTPPDT RRRGSSNEST TAPAPDDGGL GTHIDQLDNL
VQDREVSKLG LSGEGNGLQE LISLVSDETM PATAWSTHCF GTISRILSSR IRRLESLVQE
TARIQTPKRA RKPMTPVVVQ WYSAPLAGCN WNRMVVQTPQ GLEVQQFPAP PTSYSARRSP
ELSGNDIWAD LMDHDMHDPP QYNALELPPD LTNEGGVDNM GSSGRDDPIN NGFNALRLLG
INNSLSPSFI SLPRDRLSAS KLCQVYLQNV DPIIKILHRP SLSRWMVDGA PTYLGSSEDD
YAVKALESAV CYTAANTMTE HQCQAAFQKT KSSIMAVRRK MCEDALENAG LLTTRDMTVL
QAFILYLVTP TDLSKIGRRS EDKDTAVWAL VALAIRLIKA MGLNQEPSEG ARKGESFFQQ
QLRLRLWLTA CLIDLQASFA QATDPLITHR DAACAVPYVA NINDSDFDVD TAHPVASHEE
LTDTTFALVT YRVQVAGRLF NFGPGCSTAA ERHKLAQEVQ QQVFTLLHYC DPESSSYAWF
TWHSTQSIIF AVRLSELLPF RCGQPGGHVP PPSPRAEGDT TLLWRALQNL EKAQLIRADP
RGDGFRWYIT TPWLALSTAI SECNSCTDVA LVCRAWPVIE ISYRQHEELQ ISDECQLPQG
PLVHLMNKTR EKLAPLLQEG GARLSDSQTV DRASADSLQP PVPVGSIPID PLLTNGSLGA
DTAMSEASSI GSLPPFEQQC WKQMTMPTDG APVRDGVVFT SELYNPLQSD FLNSHG