BEA3_GIBF5
ID BEA3_GIBF5 Reviewed; 1301 AA.
AC S0EGU4;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=ABC transporter BEA3 {ECO:0000303|PubMed:27750383};
DE AltName: Full=Beauvericin biosynthesis cluster protein 3 {ECO:0000303|PubMed:27750383};
GN Name=BEA3 {ECO:0000303|PubMed:27750383}; ORFNames=FFUJ_09294;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
RN [2]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=27750383; DOI=10.1111/1462-2920.13576;
RA Niehaus E.M., Studt L., von Bargen K.W., Kummer W., Humpf H.U., Reuter G.,
RA Tudzynski B.;
RT "Sound of silence: the beauvericin cluster in Fusarium fujikuroi is
RT controlled by cluster-specific and global regulators mediated by H3K27
RT modification.";
RL Environ. Microbiol. 18:4282-4302(2016).
CC -!- FUNCTION: ABC transporter; part of the gene cluster that mediates the
CC biosynthesis of beauvericin (BEA), a non-ribosomal cyclic
CC hexadepsipeptide that shows antibiotic, antifungal, insecticidal, and
CC cancer cell antiproliferative and antihaptotactic activity
CC (PubMed:27750383). Functions as a regulator of beauvericin production,
CC rather than in BEA transport out of the cell (PubMed:27750383).
CC Beauvericin has low toxicity to the producing fungus and BEA3 does not
CC play a role in detoxification and self-protection of the producing
CC fungus (PubMed:27750383). {ECO:0000269|PubMed:27750383}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27750383};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is highly repressed by the histone deacetylase
CC HDA1 and the beauvericin cluster-specific repressor BEA4
CC (PubMed:27750383). BEA biosynthesis is also repressed by the activity
CC of the H3K27 methyltransferase KMT6 (PubMed:27750383).
CC {ECO:0000269|PubMed:27750383}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the production of beauvericin but
CC increases the expression of BEA1 and BEA2 (PubMed:27750383).
CC {ECO:0000269|PubMed:27750383}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR EMBL; HF679031; CCT73880.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EGU4; -.
DR SMR; S0EGU4; -.
DR STRING; 1279085.S0EGU4; -.
DR EnsemblFungi; CCT73880; CCT73880; FFUJ_09294.
DR VEuPathDB; FungiDB:FFUJ_09294; -.
DR HOGENOM; CLU_000604_17_2_1; -.
DR Proteomes; UP000016800; Chromosome 9.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 2.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 3.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1301
FT /note="ABC transporter BEA3"
FT /id="PRO_0000442148"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 745..765
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 858..878
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 880..900
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 961..981
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 987..1007
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 54..345
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 378..667
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 735..1024
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1060..1296
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413..420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1094..1101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1301 AA; 143705 MW; C1549EA95B48CD17 CRC64;
MGKRTAENSA ANGEGEEKHP EIGVDGRPEK EPTFQDYMRV FKYASKWDLL AYTVGVIASI
GVGITLPLLN IVFGQFASKF SDYAGTETLP GDEFRSKLSE LCLYLLGLFL GRLVLGYITN
FAFRMTGVRI TSAIRQDYFT ALFSQSVHVL DSMPPGYATT IITTTGNTLQ LGISEKLGVF
VEYNATMIAS IIVAFIYSWQ LSLVTFTAVV FITFSVSLVL PYITKGQTNQ TKSEAMAMSV
ASEAMSGIRM IVAYGAESRI GSKYGRFVDE AKKHAQFAGP FIALQYGLVF FSSYAAFGLA
FWYGTRLLLE DKINQLGAII VVLFSVMMIV TAMERISTPL LAVSKATVAA CEFFTVIDAP
RPEPGHLTDP DVSATEDIIL EDVTFAYPSR PHVKILDNLN LRIETGKVTA IVGPSGSGKS
TIVGLVERWY GLKDQYVISK PVEKPTDKKN NGGKEEDEQE LQELSFAGDE TGPPVDLHGR
ISTCGHSLDD INVKWWRSQI GLVQQEPFLF NDTIYSNVLN GLIGTKWENE PDEKKREMVH
EACKEAFADE FIEKLPEGYN TAVGEVGIKL SGGQRQRIAI ARAIIRRPAI LILDEATSAI
DVRGERIVQA ALDRASKNRT TIVIAHRLST IKKADRIVVL RQGQVIQSGT HEGLLTDEAG
LYYNLVNAQA LSLGEQKEGN EVIAKEERPS SVHEKAHTES TIEEKPLEKK PKNKGLLSSF
GRFFYETKSN WWMMALTLFF SACAGAAVPF QAWLFAKVII VFGYLPDESK VRSESSFWSL
MWTVLAISAG LAYCATFFLS TRTASTIRAK YQKQYFLYIL HQKVAFFDHD DHSQGTMAAR
SAEDPRQLEE LLGSNMASVF IALWTLMGTI AIALAFAWKL ALVSLCVVVP ILLAAGYWRM
RYEIKFEEMN NAVFVDSSKF ASEAIGAFRT VASFTLEVAI CDQFRTLNSN HVKDAFKKAR
WVSLLYAFSD SATIGCQAIV LYYGGRLLLS GEYDLESFFV CFMSVLNAGE TTGRALSFGP
NVAQVRAAAN RILGLRDSQV KDGPEATGEQ FISHGDGIEI ELENIYFKYP TRDVPVFDGL
SLTIEKGQFA ALVGASGSGK SSIVSLLERF YDPDHGRILC NGQDIATNNV YTYRRHLSLV
AQESSLFQGT LRENILLGVE DTVDDAAVHR VCQEASIHEF IMSLPEGYQT QVGSRGVTLS
GGQRQRVAIA RALMRNPDIL LLDEATSSLD SESEKLVQEA FERAGKGRTM VVVAHRLATV
QNADVIFVLG EGKLIEKGSH RELLAARGVY WQMCQSQALD K
