FRBG_BLOB1
ID FRBG_BLOB1 Reviewed; 1476 AA.
AC A0A0S6XH62;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=ABC-type transporter frbG {ECO:0000303|PubMed:27660098};
DE AltName: Full=FR901469 biosynthesis cluster protein G {ECO:0000303|PubMed:27660098};
GN Name=frbG {ECO:0000303|PubMed:27660098}; ORFNames=ANO11243_029910;
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, AND INDUCTION.
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).
CC -!- FUNCTION: ABC-type transporter; part of the gene cluster that mediates
CC the biosynthesis of the antifungal antibiotic FR901469, an inhibitor of
CC beta-1,3-glucansynthase, exerting antifungal activity against the
CC pathogenes Candida albicans and Aspergillus fumigatus
CC (PubMed:27660098). FR901469 is a cyclic depsipeptide containing 12
CC amino acid residues and a fatty acid chain (PubMed:27660098). Probably
CC involved in the secretion of FR901469 (Probable).
CC {ECO:0000269|PubMed:27660098, ECO:0000305|PubMed:27660098}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor frbF. {ECO:0000269|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 ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; DF938583; GAM84988.1; -; Genomic_DNA.
DR STRING; 1603295.A0A0S6XH62; -.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000054361; Unassembled WGS sequence.
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 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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1476
FT /note="ABC-type transporter frbG"
FT /id="PRO_0000454576"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 936..956
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1017..1037
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1121..1141
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1151..1171
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 274..553
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 619..845
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 898..1179
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1216..1447
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 652..659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1250..1257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1476 AA; 161215 MW; 8004588891B3F468 CRC64;
MCSIADLDGI GPFSSNPQCG HLSFTLLFEE AVLAAVPLGL CVVLALLRVR QLRLQSPKAR
RDRLYYAKLT ALFLLASVQL VQLIQWTRPS TPKTRASIAI AAVSFASTIV FIGLCHLEHI
RSAKPSDLLT LYFVTCIAFD IIRTRTLWIV SGGTAVASTF TVGLVLRLLF ALLESRPKTR
ALQRQYLRES PEARTSLINR LFFWWVNPLL WTGFKRILDP GHLFNLDRHI SSSHLFHVSA
QRLNDTDLSK SYAVLLLCLR EYKWTFLAGV LPRLALTGFT FAQPFLVTRF LSYESNRDAR
DAGATGTWLI VAYAGVYIGI AISQAGYIHQ TFRFITMVRG SLLTLLYHDT MNKGSSAGID
PTSAELTLVS ADIEKIQMGL QTMHQAWASF VDICLATWLL ERHLGLATIP SVGFSLLCVV
FGGGVAVMAG SRQTLWLEAI QKRLGLTSDV INMFKSVKMT ALVNISAARV LELRDKEITV
SKKFRRCLVF MVSLTYLSNV FAPIIGFTTY TLAPAIHKNN ILDSARAFSS LTIFALLTEG
VGSFVHSAVN LMLAVSSFER YRTTLLEKHT WHESKKASRR WTLTAPPLLE NTDAEQWALE
VLAATADAHT PPDDKQVCIQ ARDTNIGWSS EKIVVQSLSL VVRKREITLV TGPTNSGKST
LLRAMLGEAW IEGPALHRHF DRAAYCDQIP WLANKTIRQN ILGGSPVDED WYETTLQACQ
LKPDLGRLAQ GDQTVVGNEG SRLSGGQRTR VALARAVYSR LDIMLLDDIT SGLDPNTTKS
IVEALFGKDG LFRRAGQTVV VASNNASFLS LADQVVDLGS GSPKVTRRNV ESSSPVTAHV
HNQTSPKGSR IDSARGSLDE ISVADFRLEE PKREPRRLDS DTSIYMYYVR TVGVVNTAVF
LALCMALVFA MVFPSIWVAW WVEANARGET NQLAKYLLVY FFLGVAALIA LIGGGSHLML
RMVPRSARIL HRALLDAVVV APVPFMTRND AGETLNRFSQ DLEIIDTDVP LSGFTTLFAF
ITCIAQAIVV CVSSPFVTAG MVPTLVLVYF IQKFYLRTSP QLRALDLEAK APLIGHMQET
LRGLATIRAF GWAEDYEERN MRLVDESQKP FYQLTCIQRW LGLVLDLVVA GIAILLAIVI
VSDKNGGATS GFLGIALTSL VSFGLNLGGF IGGWTGLETA LTAVARVKRF SADTAKEDLP
EECQTPPTDW PQRGEIVFDD VTASYGPGTT DVLSNVSFRI SPGEKIGIIG RTGSGKSSLV
STLSRTLDLI SGSILIDSIP LSSLPRDTVR QALINMPQDA FVLHGSIRTN VDPRSRLTDE
AITEVLTELG LWPILAPLGG LDADAVSALP AQGLKQLLCF ARVLAQPGRV MVLDEATSRL
DPEASAKVKQ AIMRRSEGRT LLTVAHKIDE LDGYDRIMVV DAGKVVAFDT PGAVQGYLSS
SSPTSSPTCS SSAAALSSGA HRVAAVGVLG TEAGRA
