XYLE_ECO57
ID XYLE_ECO57 Reviewed; 491 AA.
AC P0AGF5; P09098;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=D-xylose-proton symporter {ECO:0000250|UniProtKB:P0AGF4};
DE AltName: Full=D-xylose transporter {ECO:0000250|UniProtKB:P0AGF4};
GN Name=xylE; OrderedLocusNames=Z5629, ECs5014;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Uptake of D-xylose across the boundary membrane with the
CC concomitant transport of protons into the cell (symport system).
CC {ECO:0000250|UniProtKB:P0AGF4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylose(in) + H(+)(in) = D-xylose(out) + H(+)(out);
CC Xref=Rhea:RHEA:28959, ChEBI:CHEBI:15378, ChEBI:CHEBI:53455;
CC Evidence={ECO:0000250|UniProtKB:P0AGF4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28961;
CC Evidence={ECO:0000250|UniProtKB:P0AGF4};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AGF4}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0AGF4}.
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; AE005174; AAG59230.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38437.1; -; Genomic_DNA.
DR PIR; B86096; B86096.
DR PIR; F91255; F91255.
DR RefSeq; NP_313041.1; NC_002695.1.
DR RefSeq; WP_001097274.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AGF5; -.
DR SMR; P0AGF5; -.
DR STRING; 155864.EDL933_5368; -.
DR EnsemblBacteria; AAG59230; AAG59230; Z5629.
DR EnsemblBacteria; BAB38437; BAB38437; ECs_5014.
DR GeneID; 914320; -.
DR KEGG; ece:Z5629; -.
DR KEGG; ecs:ECs_5014; -.
DR PATRIC; fig|386585.9.peg.5237; -.
DR eggNOG; COG0477; Bacteria.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_30_5_6; -.
DR OMA; VMVVFAC; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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; -; 2.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Sugar transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..491
FT /note="D-xylose-proton symporter"
FT /id="PRO_0000050295"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..55
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..133
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..200
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..312
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..369
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..442
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 168
FT /ligand="beta-D-xylose"
FT /ligand_id="ChEBI:CHEBI:28161"
FT /evidence="ECO:0000250|UniProtKB:P0AGF4"
FT BINDING 288..289
FT /ligand="beta-D-xylose"
FT /ligand_id="ChEBI:CHEBI:28161"
FT /evidence="ECO:0000250|UniProtKB:P0AGF4"
FT BINDING 294
FT /ligand="beta-D-xylose"
FT /ligand_id="ChEBI:CHEBI:28161"
FT /evidence="ECO:0000250|UniProtKB:P0AGF4"
FT BINDING 392
FT /ligand="beta-D-xylose"
FT /ligand_id="ChEBI:CHEBI:28161"
FT /evidence="ECO:0000250|UniProtKB:P0AGF4"
FT BINDING 415
FT /ligand="beta-D-xylose"
FT /ligand_id="ChEBI:CHEBI:28161"
FT /evidence="ECO:0000250|UniProtKB:P0AGF4"
SQ SEQUENCE 491 AA; 53608 MW; 2AF1AF9756C0B722 CRC64;
MNTQYNSSYI FSITLVATLG GLLFGYDTAV ISGTVESLNT VFVAPQNLSE SAANSLLGFC
VASALIGCII GGALGGYCSN RFGRRDSLKI AAVLFFISGV GSAWPELGFT SINPDNTVPV
YLAGYVPEFV IYRIIGGIGV GLASMLSPMY IAELAPAHIR GKLVSFNQFA IIFGQLLVYC
VNYFIARSGD ASWLNTDGWR YMFASECIPA LLFLMLLYTV PESPRWLMSR GKQEQAEGIL
RKIMGNTLAT QAVQEIKHSL DHGRKTGGRL LMFGVGVIVI GVMLSIFQQF VGINVVLYYA
PEVFKTLGAS TDIALLQTII VGVINLTFTV LAIMTVDKFG RKPLQIIGAL GMAIGMFSLG
TAFYTQAPGI VALLSMLFYV AAFAMSWGPV CWVLLSEIFP NAIRGKALAI AVAAQWLANY
FVSWTFPMMD KNSWLVAHFH NGFSYWIYGC MGVLAALFMW KFVPETKGKT LEELEALWEP
ETKKTQQTAT L
