ID   MMF1_PSEA3              Reviewed;         542 AA.
AC   M9M5N8;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=MFS-type efflux pump MMF1 {ECO:0000303|PubMed:23558529};
DE   AltName: Full=Mannosylerythritol lipids (MELs) biosynthesis cluster protein MMF1 {ECO:0000303|PubMed:31923270};
GN   Name=MMF1 {ECO:0000303|PubMed:23558529}; ORFNames=PANT_19d00004;
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP   FUNCTION.
RC   STRAIN=T-34;
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(2013).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=16233292; DOI=10.1263/jbb.94.187;
RA   Kitamoto D., Isoda H., Nakahara T.;
RT   "Functions and potential applications of glycolipid biosurfactants--from
RT   energy-saving materials to gene delivery carriers.";
RL   J. Biosci. Bioeng. 94:187-201(2002).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=17428643; DOI=10.1016/j.colsurfb.2007.03.003;
RA   Ito S., Imura T., Fukuoka T., Morita T., Sakai H., Abe M., Kitamoto D.;
RT   "Kinetic studies on the interactions between glycolipid biosurfactant
RT   assembled monolayers and various classes of immunoglobulins using surface
RT   plasmon resonance.";
RL   Colloids Surf. B Biointerfaces 58:165-171(2007).
RN   [4]
RP   BIOTECHNOLOGY.
RX   PubMed=17279642; DOI=10.1021/la0620814;
RA   Imura T., Hikosaka Y., Worakitkanchanakul W., Sakai H., Abe M., Konishi M.,
RA   Minamikawa H., Kitamoto D.;
RT   "Aqueous-phase behavior of natural glycolipid biosurfactant
RT   mannosylerythritol lipid A: sponge, cubic, and lamellar phases.";
RL   Langmuir 23:1659-1663(2007).
RN   [5]
RP   BIOTECHNOLOGY.
RX   PubMed=19341364; DOI=10.1042/ba20090033;
RA   Morita T., Fukuoka T., Imura T., Kitamoto D.;
RT   "Production of glycolipid biosurfactants by basidiomycetous yeasts.";
RL   Biotechnol. Appl. Biochem. 53:39-49(2009).
RN   [6]
RP   BIOTECHNOLOGY.
RX   DOI=10.1016/j.cocis.2009.05.009;
RA   Kitamoto D., Morita T., Fukuoka T., Konishi M., Imura T.;
RT   "Self-assembling properties of glycolipid biosurfactants and their
RT   potential applications.";
RL   Curr. Opin. Colloid Interface Sci. 14:315-328(2009).
RN   [7]
RP   FUNCTION.
RX   PubMed=31923270; DOI=10.1371/journal.pone.0227295;
RA   Wada K., Koike H., Fujii T., Morita T.;
RT   "Targeted transcriptomic study of the implication of central metabolic
RT   pathways in mannosylerythritol lipids biosynthesis in Pseudozyma antarctica
RT   T-34.";
RL   PLoS ONE 15:E0227295-E0227295(2020).
CC   -!- FUNCTION: Glycosyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of mannosylerythritol lipids (MELs), surface-active
CC       substances that enhance the availability of water-insoluble substrates
CC       (Probable) (PubMed:31923270). MMF1 is directly involved in the
CC       secretiopn of MALs (Probable). {ECO:0000269|PubMed:31923270,
CC       ECO:0000305|PubMed:23558529}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:31923270};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is induced when cells are grown in cultures
CC       containing vegetable oil as the carbon source.
CC       {ECO:0000269|PubMed:31923270}.
CC   -!- BIOTECHNOLOGY: MELs not only have high potential as eco-friendly
CC       biosurfactants due to their excellent surface activity, but also have
CC       attracted considerable recent interest because of thei runique
CC       properties, including self-assembly, anti-tumor and cell
CC       differentiation induction activities, and moisturizing and hair-
CC       repairing properties. {ECO:0000269|PubMed:16233292,
CC       ECO:0000269|PubMed:17279642, ECO:0000269|PubMed:17428643,
CC       ECO:0000269|PubMed:19341364, ECO:0000269|Ref.6}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; DF196785; GAC75890.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9M5N8; -.
DR   SMR; M9M5N8; -.
DR   EnsemblFungi; GAC75890; GAC75890; PANT_19d00004.
DR   OrthoDB; 672661at2759; -.
DR   Proteomes; UP000011976; 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; Transport.
FT   CHAIN           1..542
FT                   /note="MFS-type efflux pump MMF1"
FT                   /id="PRO_0000449542"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   542 AA;  58464 MW;  A3D6156AF39A387F CRC64;
     MDDKIALTSN DGERPRMKKD WRFWTIFAAL MLIAFLAALD MTMISTALPA IVAALPPSSI
     AANWITSAFL LPMVASQPIF GGLSCSLGRK NSVISALVIF LVGSIVCATA KSVLVLVVGR
     GVQGLGGGGI HALSEIIMSD LTTLRERGVY FGLIALVFAV AGFIAPVLGG VFSHSSWPWI
     FWINLPIGAV ALVLLVLFLN IRVPLLTGRQ KWEKLDLVGN AILFGSVTAV LIAVTEGGIK
     YRWSDARVWV PLVVGLIGLV AFLMVEWIPG PLCRQPVFPR DLFANRTAAV AYLQTFLHGV
     IFYGIIYMVP IYFQAIKDRT PLQSAIWSFP LTAPSTPLAL IAGLLISISG RYKKLIFIGW
     ALMAGGVGWL THWSVGTSKA EWAISQIIAG AGIGIMFPIT LPPIQASLPV ERLEAATAAY
     AFSRTFGAVW GITGATTIFA TQAAKKLRPD YGQLEPLGLN DFTVIAFAES LRYLPEQLQV
     LVKKVYADAI SDSFWLFVPL AIIGFASTFL LKDLPLPDFI KSQAVLEEKG ASENASPPES
     LA