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
