CALB_PENDC
ID CALB_PENDC Reviewed; 562 AA.
AC A0A1V6PBC8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=MFS-type transporter calB {ECO:0000303|PubMed:30598828};
DE AltName: Full=Calbistrin biosynthesis cluster protein B {ECO:0000303|PubMed:30598828};
GN Name=calB {ECO:0000303|PubMed:30598828}; ORFNames=PENDEC_c013G07044;
OS Penicillium decumbens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11843;
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=8436557; DOI=10.7164/antibiotics.46.34;
RA Jackson M., Karwowski J.P., Humphrey P.E., Kohl W.L., Barlow G.J.,
RA Tanaka S.K.;
RT "Calbistrins, novel antifungal agents produced by Penicillium restrictum.
RT I. Production, taxonomy of the producing organism and biological
RT activity.";
RL J. Antibiot. 46:34-38(1993).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=24287995; DOI=10.3390/molecules181214629;
RA Bladt T.T., Duerr C., Knudsen P.B., Kildgaard S., Frisvad J.C.,
RA Gotfredsen C.H., Seiffert M., Larsen T.O.;
RT "Bio-activity and dereplication-based discovery of ophiobolins and other
RT fungal secondary metabolites targeting leukemia cells.";
RL Molecules 18:14629-14650(2013).
RN [4]
RP IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=30598828; DOI=10.1186/s40694-018-0063-4;
RA Grijseels S., Pohl C., Nielsen J.C., Wasil Z., Nygaard Y., Nielsen J.,
RA Frisvad J.C., Nielsen K.F., Workman M., Larsen T.O., Driessen A.J.M.,
RA Frandsen R.J.N.;
RT "Identification of the decumbenone biosynthetic gene cluster in Penicillium
RT decumbens and the importance for production of calbistrin.";
RL Fungal Biol. Biotechnol. 5:18-18(2018).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of calbistrin A and related compounds. Calbistrin A is
CC a secondary metabolite with an interesting structure that was recently
CC found to have bioactivity against leukemia cells. It consists of two
CC polyketides linked by an ester bond: a bicyclic decalin containing
CC polyketide and a linear 12 carbon dioic acid structure
CC (PubMed:30598828). Required for the secretion of calbistrin A and
CC calbistrin C, as well as of related compounds decumbenone A, B and C
CC (PubMed:30598828). {ECO:0000269|PubMed:30598828}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30598828};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced in complex medium (Czapek yeast
CC autolysate medium) supporting calbistrin production (PubMed:30598828).
CC Expression is positively regulated by the calbistrin biosynthesis
CC cluster-specific transcription factor calC (PubMed:30598828).
CC {ECO:0000269|PubMed:30598828}.
CC -!- DISRUPTION PHENOTYPE: Leads to an almost complete absence of calbistrin
CC A and calbistrin C, and a decreased abundance of decumbenone A, B and C
CC in the extracellular medium. {ECO:0000269|PubMed:30598828}.
CC -!- BIOTECHNOLOGY: Calbistrin A has been reported to possess a number of
CC interesting bioactivities including antifungal active against Candida
CC albicans and cytotoxic toward both healthy and leukemic human cells.
CC {ECO:0000269|PubMed:24287995, ECO:0000269|PubMed:8436557}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; MDYL01000013; OQD73972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PBC8; -.
DR OMA; GLWERRM; -.
DR OrthoDB; 1134151at2759; -.
DR Proteomes; UP000191522; 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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..562
FT /note="MFS-type transporter calB"
FT /id="PRO_0000446478"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 562 AA; 59520 MW; 06C24CA3FB224894 CRC64;
MDEVTRTAQR SPSITETHAG ETKLAGPGEK EGDVESPVDP SADSEQNRQQ ITGLQLFAIL
ASVTLSAFLM LLDGSIIGVA IPNITSQFHS IDDIGWYTAA YQLASAALQP LSGKIYSSFS
TKWTYLFFFG LFELGSLICG VANSSSMLIG GRAVAGLGSS GLLNGGMTII AGAVPLEKRP
VYTGIYLGIS QLGIVCGPLI GGALTEYTTW RWCFYINLPV GAVTAILLLF LQVPELTEKP
RFTFALVRRV IPELDLIGFT LFAPAAIMVL LALYYGGNDF PWDSSQVIGL FCGAGVTIIV
FALWERRVGD RAMIPPSMVS HRIVYTSAIN GAALVASILV AAQYLPIYFQ GVRGYGPAMS
GVNTLPGILS QLLTVILSGV LVQKVGYYLP FAAAGSAISA VGNGIVTLFS PTTPTAKWIG
YQIVLGSGRG IGMQMGIIAI QNLLPPEKIS VGIAFMIFCQ NFAGAIFVVV GEVIFTQQLV
KQIQAHAPSV KVDAALAAGA SSSSLRALVP PGSPELQGVL LAFSNSVDRV FYLLMSLSLA
GFVAAFGMGW VDTRKKNKSE TE
