ID   SWEET_LEPBP             Reviewed;          85 AA.
AC   B0SR19;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Sugar transporter SemiSWEET;
GN   OrderedLocusNames=LEPBI_I1613 {ECO:0000312|EMBL:ABZ97720.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=456481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris {ECO:0000312|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
RN   [2] {ECO:0007744|PDB:4QNC}
RP   X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION,
RP   SUBUNIT, AND MUTAGENESIS OF TRP-48 AND ASN-64.
RX   PubMed=25186729; DOI=10.1038/nature13670;
RA   Xu Y., Tao Y., Cheung L.S., Fan C., Chen L.Q., Xu S., Perry K.,
RA   Frommer W.B., Feng L.;
RT   "Structures of bacterial homologues of SWEET transporters in two distinct
RT   conformations.";
RL   Nature 515:448-452(2014).
CC   -!- FUNCTION: The homodimer mediates transmembrane sugar transport down a
CC       concentration gradient. Transport is probably effected by rocking-type
CC       movements, where a cargo-binding cavity opens first on one and then on
CC       the other side of the membrane. {ECO:0000269|PubMed:25186729}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25186729}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25186729};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:25186729}.
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DR   EMBL; CP000786; ABZ97720.1; -; Genomic_DNA.
DR   RefSeq; WP_012388598.1; NC_010602.1.
DR   PDB; 4QNC; X-ray; 2.39 A; A/B=1-85.
DR   PDB; 5UHQ; X-ray; 2.78 A; A/B/C/D=1-85.
DR   PDB; 5UHS; X-ray; 2.80 A; A/B=1-85.
DR   PDBsum; 4QNC; -.
DR   PDBsum; 5UHQ; -.
DR   PDBsum; 5UHS; -.
DR   AlphaFoldDB; B0SR19; -.
DR   SMR; B0SR19; -.
DR   DIP; DIP-61074N; -.
DR   STRING; 456481.LEPBI_I1613; -.
DR   KEGG; lbi:LEPBI_I1613; -.
DR   HOGENOM; CLU_135915_1_1_12; -.
DR   OMA; WIIYGYK; -.
DR   OrthoDB; 1844907at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS07960-MON; -.
DR   Proteomes; UP000001847; Chromosome I.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005355; F:glucose transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:1904659; P:glucose transmembrane transport; IMP:UniProtKB.
DR   InterPro; IPR006603; PQ-loop_rpt.
DR   Pfam; PF04193; PQ-loop; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Membrane; Reference proteome; Sugar transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..85
FT                   /note="Sugar transporter SemiSWEET"
FT                   /id="PRO_0000432577"
FT   TRANSMEM        5..25
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000269|PubMed:25186729"
FT   TRANSMEM        33..53
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000269|PubMed:25186729"
FT   TRANSMEM        57..77
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000269|PubMed:25186729"
FT   DOMAIN          2..59
FT                   /note="PQ-loop"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         48
FT                   /note="W->A: Impairs glucose transport."
FT                   /evidence="ECO:0000269|PubMed:25186729"
FT   MUTAGEN         64
FT                   /note="N->A: Impairs glucose transport."
FT                   /evidence="ECO:0000269|PubMed:25186729"
FT   HELIX           2..15
FT                   /evidence="ECO:0007829|PDB:4QNC"
FT   HELIX           17..27
FT                   /evidence="ECO:0007829|PDB:4QNC"
FT   TURN            29..32
FT                   /evidence="ECO:0007829|PDB:5UHQ"
FT   HELIX           35..55
FT                   /evidence="ECO:0007829|PDB:4QNC"
FT   HELIX           58..79
FT                   /evidence="ECO:0007829|PDB:4QNC"
SQ   SEQUENCE   85 AA;  9845 MW;  2CBD5FB6C9162822 CRC64;
     MENLIGYVAA FLTTVSFLPQ VLRVVMTKQT RDISRNMYIM FFLGVVLWFV YGILRSDLPI
     ILANVVTLFF VTIILYYKLT EGNQT