ID   BRAE_ANNTR              Reviewed;        1481 AA.
AC   P9WER4; A0A866WM10;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=ABC-type transporter braE {ECO:0000303|PubMed:32936132};
DE   AltName: Full=Brasilane terpene glycosides biosynthesis cluster protein E {ECO:0000303|PubMed:32936132};
GN   Name=braE {ECO:0000303|PubMed:32936132};
OS   Annulohypoxylon truncatum (Hypoxylon truncatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Annulohypoxylon.
OX   NCBI_TaxID=327061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=DSM 103480 / CBS 140778;
RX   PubMed=32936132; DOI=10.1039/d0cc03950k;
RA   Feng J., Surup F., Hauser M., Miller A., Wennrich J.P., Stadler M.,
RA   Cox R.J., Kuhnert E.;
RT   "Biosynthesis of oxygenated brasilane terpene glycosides involves a
RT   promiscuous N-acetylglucosamine transferase.";
RL   Chem. Commun. (Camb.) 56:12419-12422(2020).
CC   -!- FUNCTION: ABC-type transporter; part of the gene cluster that mediates
CC       the biosynthesis of the brasilane terpene glycosides brasilane D and E.
CC       {ECO:0000269|PubMed:32936132}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC       Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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; MT383109; QOE88887.1; -; Genomic_DNA.
DR   SMR; P9WER4; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR   CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR   Gene3D; 1.20.1560.10; -; 2.
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; IPR044746; ABCC_6TM_D1.
DR   InterPro; IPR044726; ABCC_6TM_D2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
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   3: Inferred from homology;
KW   ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1481
FT                   /note="ABC-type transporter braE"
FT                   /id="PRO_0000453907"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        887..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        928..948
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        1001..1021
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        1026..1046
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        1111..1131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        1144..1164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   DOMAIN          281..549
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          594..823
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          887..1166
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1224..1477
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         627..634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1260..1267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        671
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        813
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1481 AA;  162826 MW;  82633C0802973149 CRC64;
     MLFSACADTN DQSLGPNVLG CRGDFDFTVK FEQLCFSLTP AAIFILASPW RVAHLVRKPT
     IVGAPLLRLA KLGVLVSYAS LELSQLILIT VLPFGASGID IISSALRLAA ALCMVGLSYF
     DHSKSPRPSI FLSAYLFFTL LFDIAQARTY WLASSTRPEI AFTAIFTAAL AMKIAMLLLE
     AQRKTKWVAW DSKDHSPEET SGIYTLGVFS WLNKLFFDGY HKTLGIRDLY PLDQNLAATH
     LSERFSRHIN EAKRKGHEIG LMEALAKTLY VPMILPIPAK LAAIGSFFCQ PLFISSLTSR
     LSQSEPVPAN IGYGFIGASI CIYSVIAISQ SLYWYFQQRL LYMMRACLAT AIYTKTTEAR
     AADEDENASL TLMSIDIERI MKGSLYMHEL WGNVIEVALS AWLLYNLLGV AFIAPIVVVC
     ICVGGVSFFM RFMGDSQRNW MAGIQKRVGL TSSVIGNMKN IKISGLTSPI SRFVEKLRVD
     ELQAGSNFRL LMLTCSVFAY IPLLLSPPIT FGVARRSLDA TKLFTSLSYL LLMSTPLQNL
     LETLPQMAAA VACLGRIQKF LQGEGRDDYR IFLAGSRRDP EKPSLDQLDK SPAVAIKDGS
     FGWKPDKMVL NNLDVEIPRG SLTIVVGPIA SGKSSLCKAL LGEMPHSQGT VTIATKFSCV
     GYCDQTPFLS NGSIRDNIIG YSPFDAQRYA EVVDGTMLGI DFETLPEADR TNIGSNGITL
     SGGQKQRVSL ARCLYLQSDL LIMDDVFSGL DADTEDQVFQ RVFGANGILK RRQATVVLCT
     HSVRHIPSAT HVIALSTDGT VVEQGTFGDL VANQSYIHSL GVKAPSTSQA DSEKIESDDS
     AIEPQINLIE RAPTETPEVG VNDKSRLSGD SAAYIVYMKS MGTMLPIAIF TSGLLYGFFY
     NFPTIWLTYW SADAVATNPS HSFGYYAAIY AVLEVCAMLS LIWLGVLLYI TVLTRSGVSL
     HHAALRTLIH APLRFFTTTD QGIITNLFSQ DLSLIDNELP SALLNVIYMV FVGIGQAAVI
     ASSSPYLAIS YPFLFGMLYV VQKFYLRTSR QLRLLDLEAK SPLYTHFLDT SKGIVTLRAF
     GFVSEDRAKN AFLLDTSQRP AYLLAMIQQW LHFVLNVVVA IIAVMLTSLA VRLRSNSGFT
     GASLVTLMSF GEMLSGVVIY YTALETSLGA ISRLKAFDKA AKTETKDGED IVPPEEWPPR
     GEIILNNVSA SYEYELPLFL SIRLTTNELS SNDTQPETPT LALKNLRLRI RPGEKIAICG
     RTGSGKSSLI SLLLKLLDPI DETLDCVNID NTPLSRIDRV TLRQRIIAIP QDIVFLPDGS
     TFQENLDPSN VSTAADAQAV LEAVDLWDFV RDKGGLEAGM TVSNLSQGQR QLFSLGRAVL
     RRRIRARSLG LGGGGSEGGI LLLDEVSSSV DRETEKAMQE VIRVEFREYT VVAVSHRLDI
     IMDYDRVVVM EKGEIVEEGN PARLVEEPGT RFGELWSVGG N