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XYLT_LEVBR
ID   XYLT_LEVBR              Reviewed;         457 AA.
AC   O52733;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=D-xylose transporter {ECO:0000303|PubMed:9835554};
DE   AltName: Full=D-xylose-proton symporter {ECO:0000303|PubMed:9835554};
GN   Name=xylT {ECO:0000303|PubMed:9835554};
OS   Levilactobacillus brevis (Lactobacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=1580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX   PubMed=9835554; DOI=10.1128/aem.64.12.4720-4728.1998;
RA   Chaillou S., Bor Y.-C., Batt C.A., Postma P.W., Pouwels P.H.;
RT   "Molecular cloning and functional expression in Lactobacillus plantarum 80
RT   of xylT, encoding the D-xylose-H+ symporter of Lactobacillus brevis.";
RL   Appl. Environ. Microbiol. 64:4720-4728(1998).
CC   -!- FUNCTION: Uptake of D-xylose across the boundary membrane with the
CC       concomitant transport of protons into the cell (symport system).
CC       Transport is driven by the proton motive force generated by either
CC       malolactic fermentation or by the metabolism of D-glucose.
CC       {ECO:0000269|PubMed:9835554}.
CC   -!- ACTIVITY REGULATION: Transport is inhibited by 6-deoxy-D-glucose.
CC       {ECO:0000269|PubMed:9835554}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=215 uM for D-xylose {ECO:0000269|PubMed:9835554};
CC         Vmax=35 nmol/min/mg enzyme {ECO:0000269|PubMed:9835554};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: By D-xylose. {ECO:0000269|PubMed:9835554}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR   EMBL; AF045552; AAC95127.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52733; -.
DR   SMR; O52733; -.
DR   TCDB; 2.A.1.1.41; the major facilitator superfamily (mfs).
DR   PRIDE; O52733; -.
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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Sugar transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..457
FT                   /note="D-xylose transporter"
FT                   /id="PRO_0000050296"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         138
FT                   /ligand="beta-D-xylose"
FT                   /ligand_id="ChEBI:CHEBI:28161"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGF4"
FT   BINDING         254..255
FT                   /ligand="beta-D-xylose"
FT                   /ligand_id="ChEBI:CHEBI:28161"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGF4"
FT   BINDING         260
FT                   /ligand="beta-D-xylose"
FT                   /ligand_id="ChEBI:CHEBI:28161"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGF4"
FT   BINDING         362
FT                   /ligand="beta-D-xylose"
FT                   /ligand_id="ChEBI:CHEBI:28161"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGF4"
FT   BINDING         385
FT                   /ligand="beta-D-xylose"
FT                   /ligand_id="ChEBI:CHEBI:28161"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGF4"
SQ   SEQUENCE   457 AA;  49199 MW;  E097EB2B67A92F67 CRC64;
     MRKVSTGFVY FFGALGGLLF GYDTGVISGA ILFIQKQMNL GSWQQGWVVS AVLLGAILGA
     AIIGPSSDRF GRRKLLLLSA IIFFVGALGS AFSPEFWTLI ISRIILGMAV GAASALIPTY
     LAELAPSDKR GTVSSLFQLM VMTGILLAYI TNYSFSGFYT GWRWMLGFAA IPAALLFLGG
     LILPESPRFL VKSGHLDEAR HVLDTMNKHD QVAVNKEIND IQESAKIVSG GWSELFGKMV
     RPSLIIGIGL AIFQQVMGCN TVLYYAPTIF TDVGFGVSAA LLAHIGIGIF NVIVTAIAVA
     IMDKIDRKKI VNIGAVGMGI SLFVMSIGMK FSGGSQTAAI ISVIALTVYI AFFSATWGPV
     MWVMIGEVFP LNIRGLGNSF ASVINWTANM IVSLTFPSLL DFFGTGSLFI GYGILCFASI
     WFVQKKVFET RNRSLEDIEA TLRAKTGEDA AELSTTK
 
 
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