XYLE_ECOLI
ID XYLE_ECOLI Reviewed; 491 AA.
AC P0AGF4; P09098; Q2M6S3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=D-xylose-proton symporter;
DE AltName: Full=D-xylose transporter;
GN Name=xylE; OrderedLocusNames=b4031, JW3991;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2820984; DOI=10.1016/s0021-9258(18)47883-0;
RA Davis E.O., Henderson P.J.F.;
RT "The cloning and DNA sequence of the gene xylE for xylose-proton symport in
RT Escherichia coli K12.";
RL J. Biol. Chem. 262:13928-13932(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3543693; DOI=10.1038/325641a0;
RA Maiden M.C.J., Davis E.O., Baldwin S.A., Moore D.C.M., Henderson P.J.F.;
RT "Mammalian and bacterial sugar transport proteins are homologous.";
RL Nature 325:641-643(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
RC STRAIN=K12;
RX PubMed=2836810; DOI=10.1093/nar/16.9.4097;
RA Francoz E., Dassa E.;
RT "3' end of the malEFG operon in E.coli: localization of the transcription
RT termination site.";
RL Nucleic Acids Res. 16:4097-4109(1988).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8] {ECO:0007744|PDB:4GBY, ECO:0007744|PDB:4GBZ, ECO:0007744|PDB:4GC0}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEXES WITH
RP BETA-D-XYLOPYRANOSE AND BETA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF PHE-24; GLY-83; ARG-133;
RP GLU-153; ARG-160; GLN-168; GLN-288; GLN-289; ASN-294; TYR-298; ASN-325;
RP GLY-340; ARG-341; TRP-392; GLU-397; ARG-404 AND TRP-416.
RX PubMed=23075985; DOI=10.1038/nature11524;
RA Sun L., Zeng X., Yan C., Sun X., Gong X., Rao Y., Yan N.;
RT "Crystal structure of a bacterial homologue of glucose transporters GLUT1-
RT 4.";
RL Nature 490:361-366(2012).
RN [9] {ECO:0007744|PDB:4JA3, ECO:0007744|PDB:4JA4}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS).
RX PubMed=23624861; DOI=10.1038/nsmb.2569;
RA Quistgaard E.M., Low C., Moberg P., Tresaugues L., Nordlund P.;
RT "Structural basis for substrate transport in the GLUT-homology family of
RT monosaccharide transporters.";
RL Nat. Struct. Mol. Biol. 20:766-768(2013).
CC -!- FUNCTION: Uptake of D-xylose across the boundary membrane with the
CC concomitant transport of protons into the cell (symport system).
CC Glucose is not transported, but can compete for xylose binding sites
CC and can inhibit xylose transport (in vitro).
CC {ECO:0000269|PubMed:23075985}.
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:0000269|PubMed:23075985};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28961;
CC Evidence={ECO:0000269|PubMed:23075985};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:23075985}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23075985}.
CC -!- INDUCTION: By xylose.
CC -!- MISCELLANEOUS: E.coli has two D-xylose transport systems that
CC accumulate sugar against a concentration gradient: the XylE system
CC which utilizes the electrochemical gradient of protons and that is
CC insensitive to cold osmotic shock and the XylF system that uses a high-
CC energy phosphate compound and is sensitive to cold osmotic shock.
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; J02812; AAA79016.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43125.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77001.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78033.1; -; Genomic_DNA.
DR EMBL; X06663; CAA29863.1; -; Genomic_DNA.
DR PIR; A26430; A26430.
DR RefSeq; NP_418455.1; NC_000913.3.
DR RefSeq; WP_001097274.1; NZ_LN832404.1.
DR PDB; 4GBY; X-ray; 2.81 A; A=1-491.
DR PDB; 4GBZ; X-ray; 2.89 A; A=1-491.
DR PDB; 4GC0; X-ray; 2.60 A; A=1-491.
DR PDB; 4JA3; X-ray; 3.80 A; A/B=2-485.
DR PDB; 4JA4; X-ray; 4.20 A; A/B/C=2-485.
DR PDB; 4QIQ; X-ray; 3.51 A; A=6-480.
DR PDB; 6N3I; X-ray; 3.69 A; A=1-491.
DR PDBsum; 4GBY; -.
DR PDBsum; 4GBZ; -.
DR PDBsum; 4GC0; -.
DR PDBsum; 4JA3; -.
DR PDBsum; 4JA4; -.
DR PDBsum; 4QIQ; -.
DR PDBsum; 6N3I; -.
DR AlphaFoldDB; P0AGF4; -.
DR SMR; P0AGF4; -.
DR BioGRID; 4262660; 13.
DR STRING; 511145.b4031; -.
DR TCDB; 2.A.1.1.3; the major facilitator superfamily (mfs).
DR jPOST; P0AGF4; -.
DR PaxDb; P0AGF4; -.
DR PRIDE; P0AGF4; -.
DR EnsemblBacteria; AAC77001; AAC77001; b4031.
DR EnsemblBacteria; BAE78033; BAE78033; BAE78033.
DR GeneID; 948529; -.
DR KEGG; ecj:JW3991; -.
DR KEGG; eco:b4031; -.
DR PATRIC; fig|1411691.4.peg.2680; -.
DR EchoBASE; EB1069; -.
DR eggNOG; COG0477; Bacteria.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_30_5_6; -.
DR InParanoid; P0AGF4; -.
DR OMA; VMVVFAC; -.
DR PhylomeDB; P0AGF4; -.
DR BioCyc; EcoCyc:XYLE-MON; -.
DR BioCyc; MetaCyc:XYLE-MON; -.
DR PRO; PR:P0AGF4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015519; F:D-xylose:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015753; P:D-xylose transmembrane transport; IDA:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Sugar transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..491
FT /note="D-xylose-proton symporter"
FT /id="PRO_0000050294"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT TRANSMEM 10..32
FT /note="Helical; Name=1"
FT TOPO_DOM 33..58
FT /note="Periplasmic"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT TOPO_DOM 80..84
FT /note="Cytoplasmic"
FT TRANSMEM 85..105
FT /note="Helical; Name=3"
FT TOPO_DOM 106..128
FT /note="Periplasmic"
FT TRANSMEM 129..150
FT /note="Helical; Name=4"
FT TOPO_DOM 151..162
FT /note="Cytoplasmic"
FT TRANSMEM 163..183
FT /note="Helical; Name=5"
FT TOPO_DOM 184..200
FT /note="Periplasmic"
FT TRANSMEM 201..221
FT /note="Helical; Name=6"
FT TOPO_DOM 222..276
FT /note="Cytoplasmic"
FT TRANSMEM 277..299
FT /note="Helical; Name=7"
FT TOPO_DOM 300..312
FT /note="Periplasmic"
FT TRANSMEM 313..334
FT /note="Helical; Name=8"
FT TOPO_DOM 335..343
FT /note="Cytoplasmic"
FT TRANSMEM 344..364
FT /note="Helical; Name=9"
FT TOPO_DOM 365..369
FT /note="Periplasmic"
FT TRANSMEM 370..390
FT /note="Helical; Name=10"
FT TOPO_DOM 391..407
FT /note="Cytoplasmic"
FT TRANSMEM 408..428
FT /note="Helical; Name=11"
FT TOPO_DOM 429..442
FT /note="Periplasmic"
FT TRANSMEM 443..463
FT /note="Helical; Name=12"
FT TOPO_DOM 464..491
FT /note="Cytoplasmic"
FT BINDING 168
FT /ligand="beta-D-xylose"
FT /ligand_id="ChEBI:CHEBI:28161"
FT /evidence="ECO:0000269|PubMed:23075985,
FT ECO:0007744|PDB:4GBY"
FT BINDING 288..289
FT /ligand="beta-D-xylose"
FT /ligand_id="ChEBI:CHEBI:28161"
FT /evidence="ECO:0000269|PubMed:23075985,
FT ECO:0007744|PDB:4GBY"
FT BINDING 294
FT /ligand="beta-D-xylose"
FT /ligand_id="ChEBI:CHEBI:28161"
FT /evidence="ECO:0000269|PubMed:23075985,
FT ECO:0007744|PDB:4GBY"
FT BINDING 392
FT /ligand="beta-D-xylose"
FT /ligand_id="ChEBI:CHEBI:28161"
FT /evidence="ECO:0000269|PubMed:23075985,
FT ECO:0007744|PDB:4GBY"
FT BINDING 415
FT /ligand="beta-D-xylose"
FT /ligand_id="ChEBI:CHEBI:28161"
FT /evidence="ECO:0000269|PubMed:23075985,
FT ECO:0007744|PDB:4GBY"
FT MUTAGEN 24
FT /note="F->A: Decreases xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 83
FT /note="G->A: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 133
FT /note="R->C,H,L: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 153
FT /note="E->A: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 160
FT /note="R->A: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 168
FT /note="Q->A: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 288
FT /note="Q->A: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 289
FT /note="Q->A: Strongly decreases xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 294
FT /note="N->A: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 298
FT /note="Y->A: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 325
FT /note="N->A: No effect on xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 340
FT /note="G->A: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 341
FT /note="R->A,W: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 392
FT /note="W->A: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 397
FT /note="E->A: Abolishes xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 404
FT /note="R->A: Strongly decreases xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT MUTAGEN 415
FT /note="Q->A: Strongly decreases xylose transport."
FT MUTAGEN 416
FT /note="W->A: Strongly decreases xylose transport."
FT /evidence="ECO:0000269|PubMed:23075985"
FT CONFLICT 64
FT /note="A -> V (in Ref. 6; CAA29863)"
FT /evidence="ECO:0000305"
FT HELIX 7..29
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 64..81
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 84..103
FT /evidence="ECO:0007829|PDB:4GC0"
FT TURN 105..109
FT /evidence="ECO:0007829|PDB:4GC0"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 126..152
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 160..186
FT /evidence="ECO:0007829|PDB:4GC0"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4GBZ"
FT TURN 191..197
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 233..266
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 311..339
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 342..364
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 369..384
FT /evidence="ECO:0007829|PDB:4GC0"
FT TURN 385..388
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 389..397
FT /evidence="ECO:0007829|PDB:4GC0"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 404..423
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 425..429
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 431..439
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 443..462
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:4GC0"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:4GC0"
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
