ID   MDL1_CANAX              Reviewed;         685 AA.
AC   P97998;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=ATP-dependent permease MDL1;
GN   Name=MDL1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=491A;
RA   McCreath K.J.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC       Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Mitochondrial peptide exporter (TC 3.A.1.212) subfamily. {ECO:0000305}.
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DR   EMBL; Y12327; CAA72996.1; -; Genomic_DNA.
DR   AlphaFoldDB; P97998; -.
DR   SMR; P97998; -.
DR   VEuPathDB; FungiDB:CAWG_01561; -.
DR   VEuPathDB; FungiDB:CR_02150W_A; -.
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   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
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; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..685
FT                   /note="ATP-dependent permease MDL1"
FT                   /id="PRO_0000093440"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        158..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        266..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          97..407
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          440..680
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          48..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         475..482
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        553
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        576
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   685 AA;  75868 MW;  46239E214CE1267A CRC64;
     MIGMNRLIFS KAFTSSCKSV GKVPFAKSIT RANTRYFKPT SILQQIRFNS KSSTAPNTEA
     NSNGSTNSQS DTKKPRPKLT SEIFKLLRLA KPESKLIFFA LICLVTTSAT SMALPLMIGK
     IIDTTKKDDD DDKDNDNDDK DDTQPSDKLI FGLPQPQFYS ALGVLFIVSA STNFGRIYLL
     RSVGERLVAR LRSRLFSKIL AQDAYFFDLG PSKTGMKTGD LISRIASDTQ IISKSLSMNI
     SDGIRAIISG CVGLSMMCYV SWKLSLCMSL IFPPLITMSW FYGRKIKALS KLIQENIGDM
     TKVTEEKLNG VKVIQTFSQQ QSVVHSYNQE IKNIFNSSMR EAKLAGFFYS TNGFIGNVTM
     IGLLIMGTKL IGAGELTVGD LSSFMMYAVY TGTSVFGLGN FYTELMKGIG AAERVFELVE
     YQPRISNHLG KKVDELNGDI EFKGIDFTYP SRPESGIFKD LNLHIKQGEN VCLVGPSGSG
     KSTVSQLLLR FYDPEKGTIQ IGDDVITDLN LNHYRSKLGY VQQEPLLFSG TIKENILFGK
     EDATDEEINN ALNLSYASNF VRHLPDGLDT KIGASNSTQL SGGQKQRVSL ARTLIRDPKI
     LILDEATSAL DSVSEEIVMS NLIQLNKNRG VTLISIAHRL STIKNSDRII VFNQDGQIVE
     DGKFNELHND PNSQFNKLLK SHSLE