ID   SSU1_TRIRU              Reviewed;         375 AA.
AC   A3QUP1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Sulfite efflux pump SSU1;
GN   Name=SSU1;
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX   PubMed=17322211; DOI=10.1099/mic.0.2006/003335-0;
RA   Lechenne B., Reichard U., Zaugg C., Fratti M., Kunert J., Boulat O.,
RA   Monod M.;
RT   "Sulphite efflux pumps in Aspergillus fumigatus and dermatophytes.";
RL   Microbiology 153:905-913(2007).
CC   -!- FUNCTION: Sulphite efflux pump required for the secretion of sulphite
CC       as a reducing agent. In the presence of sulphite, cystine in keratin is
CC       directly cleaved to cysteine and S-sulphocysteine, and thereby, reduced
CC       proteins become accessible to hydrolysis by a variety of secreted
CC       endo- and exoproteases. Excretion of sulphite mediated by an efflux
CC       pump represents also an detoxification pathway for dermatophytes during
CC       infection of the epidermal stratum corneum, hair and nails, which are
CC       rich in cysteine. {ECO:0000269|PubMed:17322211}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Expression is strongly increased during growth on protein
CC       rich medium containing keratin or cystine-arginine.
CC       {ECO:0000269|PubMed:17322211}.
CC   -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate
CC       transporter (TDT) family. {ECO:0000305}.
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DR   EMBL; DQ777768; ABG88187.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3QUP1; -.
DR   SMR; A3QUP1; -.
DR   VEuPathDB; FungiDB:TERG_02694; -.
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:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.50.10.150; -; 1.
DR   InterPro; IPR004695; SLAC1/Mae1/Ssu1/TehA.
DR   InterPro; IPR038665; Voltage-dep_anion_channel_sf.
DR   Pfam; PF03595; SLAC1; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..375
FT                   /note="Sulfite efflux pump SSU1"
FT                   /id="PRO_0000384415"
FT   TOPO_DOM        1..25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..59
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..101
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..135
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..167
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..200
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..234
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..277
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        299..309
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        331..343
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        365..375
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   375 AA;  41802 MW;  2A6435FC6663C699 CRC64;
     MPSGSGFHNI EEAGEKARKR DDWIAISNFH PGWFSVNMGT GITAILLQNL PYQFPGLHYI
     AVVLFILNVI IFFLFLTISI TRYCLWPDKF KAMLAHPAHS MLLGTFPMGF ATIINCIVFI
     CVPVWGEWAS RFAWGLWWID AAVSVAICYF VPFMLMTKHT SSLETMTAAW LLPIVAPVVA
     AASGGVVADS LQNDTHALIT ILVCYAMWGS AVPLAMVILV IYFQRLAIHK LVPRAAIVSA
     LLPIGPLGQG GFGLMQLGVV AKRVFPRLDF LAPIAGDIFY VMGAFIAMIM WGFGLIWLWF
     ALASFTRGKF YFNIGWWAFT FPLGVFTTAT TQMGKEFNSP FFDILGTFFS IVVTCMWVLV
     FALTVYKSCT KELFR