MDR_STABO
ID MDR_STABO Reviewed; 1299 AA.
AC H6TB12;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Sophorolipid transporter {ECO:0000303|PubMed:23516968};
DE EC=7.6.2.-;
GN Name=mdr;
OS Starmerella bombicola (Yeast) (Candida bombicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Starmerella.
OX NCBI_TaxID=75736;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 22214 / CBS 6009 / JCM 9596 / NBRC 10243 / NRRL Y-17069;
RA Van Bogaert I.N.A., Soetaert W.;
RT "A sophorolipid transporter.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC STRAIN=ATCC 22214 / CBS 6009 / JCM 9596 / NBRC 10243 / NRRL Y-17069;
RX PubMed=23964782; DOI=10.1021/pr400392a;
RA Ciesielska K., Li B., Groeneboer S., Van Bogaert I., Lin Y.C., Soetaert W.,
RA Van de Peer Y., Devreese B.;
RT "SILAC-based proteome analysis of Starmerella bombicola sophorolipid
RT production.";
RL J. Proteome Res. 12:4376-4392(2013).
RN [3]
RP FUNCTION.
RX PubMed=23516968; DOI=10.1111/mmi.12200;
RA Van Bogaert I.N., Holvoet K., Roelants S.L., Li B., Lin Y.C.,
RA Van de Peer Y., Soetaert W.;
RT "The biosynthetic gene cluster for sophorolipids: a biotechnological
RT interesting biosurfactant produced by Starmerella bombicola.";
RL Mol. Microbiol. 88:501-509(2013).
CC -!- FUNCTION: Transports acidic acylated and non-acylated sophorolipids
CC (SLs) into the extracellular space, where they can be lactonized by
CC lactone esterase. {ECO:0000269|PubMed:23516968}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23516968};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Induced in early stationary phase (at protein level).
CC {ECO:0000269|PubMed:23964782}.
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; HQ660581; AET14838.1; -; Genomic_DNA.
DR AlphaFoldDB; H6TB12; -.
DR SMR; H6TB12; -.
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; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1299
FT /note="Sophorolipid transporter"
FT /id="PRO_0000443100"
FT TOPO_DOM 1..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 86..114
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 136..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 209..214
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 236..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 315..326
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 348..725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 747..769
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 770..790
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 791..848
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 849..869
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 870..874
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 875..895
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 896..954
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 955..975
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 976..987
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 988..1008
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1009..1299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 65..356
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 393..638
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 727..1016
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1053..1293
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 681..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 428..435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1088..1095
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1299 AA; 142459 MW; 011E3B5CE82303FC CRC64;
MVDDIQVEKR EKLIETKDKL LEEKLSALDP HEANVLRSQL ETKRVATSFF RLFRFCTPLD
VFLEILALFF AAVHGAALPM FTLVVGAIFN TFRDFTSYDL KGNEFQHKVN HLSLYFVYIG
IGMLGSAFLE SFLLVDRGEV LAGRYRKHYL SAVIRQNIAF YDKLGGGEVS TRIINDTNSI
QEAISDKLGN VVQGIASFIA ATVISFASQW KLACILLSAV GFMVITMGTG ATFMAKYQLR
SDAIYSQSGA TVAEEALSAV RTTVAFGAQP HLAVKYEKVL DRVVKESKRS SYSLGVMLAC
IWASTFWVYA LALWQGSREI VSGSADVGKI IVVITAMLLG SFQLGNIAPN VRFLVKGLTA
ASILNEAIDR VPVIDGQSID KGIVPQTKAV GRIELKNVKF RYPSRPDVLV LSDFSLEVPA
GSTVALVGAS GSGKSTIVGI LERFYLPLEG SVTLDGQEIS DLNTRWLRQQ IGYVQQEPVL
FSESIYENIS YGLIGTDIEF ADEHVKEAKI IQACKDANAW DFIQTLSEGI QTNVGDRGFL
LSGGQKQRIA IARAIVSDPK ILLLDEATSA LDTKSEGIVQ DALDKAAEGR TTIVVAHRLS
TIKDANKIVV MSKGNVIEQG THNELIQREG PYKALVDAQR VTKAKSTNVE VLDIEALDIS
PLDSLNEKFN PKDVSTLSVH SAGTQTTQPP EYQENDIPGV RNPPHSTLMT NTKLVWGLNR
KEWGYILIGS LASIILGYCY PAMAIITGQT TGSMVLPPSE YGKMRHVVNI MGWWYFFVGC
ISFMTAFITI AALSLASDKL VKNIRLALFR QLMRMDIAFF DHKNNTPGAL TSILAKEAKM
IEGLSGATLG QIQQSLVTLI GGIVTGIPFN WRIGLVATSV VPVMLVCGFV RVWVLTQLSD
RAREVYERSG SMASEYTSAV RTVQSLTREL DVVVKYTKTV DSQIFSSRIA IARSALYYAL
SEGMTPWVVA LVFWWGSTVM RRGEASVAGY MTVFMAIITG SQAAGQIFSY APNMNSAKDA
ARNIYRILTA TPSIDVWSEE GYVAPEESVR GDIEFRHVNF RYPTRPQVPV LQDLNLTVKK
GQYIALVGAS GCGKSTTIGL VERFYDPLAG QVLFDGKDLR EYNLNALRSH IALVQQEPML
YSGTLRENIL MGWSGPESEV TQEMIEDAAR KANIHEFIMS LPDGYETLSG SRGSLLSGGQ
KQRIAIARAL IRNPKVLLLD EATSALDSES EKVVQAALDA AAKGRTTIAV AHRLSTIQKA
DVIYVFSGGR IVEQGDHQSL LELNGWYAEL VNLQGLGEI
