SSU1_ARTBC
ID SSU1_ARTBC Reviewed; 375 AA.
AC A3R044; D4B4Y9; D4B4Z0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Sulfite efflux pump SSU1 {ECO:0000303|PubMed:17322211};
GN Name=SSU1 {ECO:0000303|PubMed:17322211};
GN ORFNames=ARB_03529 {ECO:0000303|PubMed:23353986},
GN ARB_03530 {ECO:0000303|PubMed:23353986};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23353986; DOI=10.1038/jid.2013.41;
RA Grumbt M., Monod M., Yamada T., Hertweck C., Kunert J., Staib P.;
RT "Keratin degradation by dermatophytes relies on cysteine dioxygenase and a
RT sulfite efflux pump.";
RL J. Invest. Dermatol. 133:1550-1555(2013).
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 ECO:0000269|PubMed:23353986}.
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 -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to L-cysteine and
CC sulfite. Abolishes the ability to grow on human hair and strongly
CC impairs growth on human nails. {ECO:0000269|PubMed:23353986}.
CC -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate
CC transporter (TDT) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE29634.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EFE29635.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF035480; ABM87938.1; -; mRNA.
DR EMBL; ABSU01000035; EFE29634.1; ALT_SEQ; Genomic_DNA.
DR EMBL; ABSU01000035; EFE29635.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003010274.1; XM_003010228.1.
DR RefSeq; XP_003010275.1; XM_003010229.1.
DR AlphaFoldDB; A3R044; -.
DR SMR; A3R044; -.
DR STRING; 663331.A3R044; -.
DR TCDB; 2.A.16.4.2; the telurite-resistance/dicarboxylate transporter (tdt) family.
DR EnsemblFungi; EFE29634; EFE29634; ARB_03529.
DR EnsemblFungi; EFE29635; EFE29635; ARB_03530.
DR GeneID; 9525542; -.
DR GeneID; 9525543; -.
DR KEGG; abe:ARB_03529; -.
DR KEGG; abe:ARB_03530; -.
DR eggNOG; ENOG502QT02; Eukaryota.
DR HOGENOM; CLU_030057_5_1_1; -.
DR Proteomes; UP000008866; 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: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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..375
FT /note="Sulfite efflux pump SSU1"
FT /id="PRO_0000384413"
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"
FT CONFLICT 8
FT /note="H -> Q (in Ref. 2; EFE29635/EFE29634)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 41844 MW; 094FCB8494876D87 CRC64;
MPSGSGFHNI EEAGEKARKR DDWIAISNFH PGWFSVNMGT GITAILLQNL PYQFPGLHYI
AVILFILNVI IFFLFLTISI TRYCLWPDKF KAMLAHPAHS MLLGTFPMGF ATIINCIVFI
CVPVWGEWAS RFAWGLWWID AAVSVAICYF VPFMLMTKHT SSLETMTAAW LLPIVAPVVA
AASGGVVADS LQNDTHALIT ILVCYVMWGS AVPLAMVILV IYFQRLAIHK LVPRAAIVSA
LLPIGPLGQG GFGLMQLGVV AKRVFPRLDF LAPIAGDIFY VMGAFIAMIM WGFGLIWLWF
ALASFTRGKF YFNIGWWAFT FPLGVFTTAT TQMGKEFNSP FFDILGTFFS IVVTCMWVLV
FALTVYKSCT KELFR
