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Protein

D-xylose-proton symporter

Gene

xylE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Uptake of D-xylose across the boundary membrane with the concomitant transport of protons into the cell (symport system). Glucose is not transported, but can compete for xylose binding sites and can inhibit xylose transport (in vitro).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei168 – 1681Monosaccharide
Binding sitei392 – 3921Monosaccharide
Binding sitei415 – 4151Monosaccharide

GO - Molecular functioni

  • D-xylose:proton symporter activity Source: EcoCyc

GO - Biological processi

  • D-xylose transport Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Sugar transport, Symport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:XYLE-MONOMER.
ECOL316407:JW3991-MONOMER.
MetaCyc:XYLE-MONOMER.

Protein family/group databases

TCDBi2.A.1.1.3. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
D-xylose-proton symporter
Alternative name(s):
D-xylose transporter
Gene namesi
Name:xylE
Ordered Locus Names:b4031, JW3991
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11076. xylE.

Subcellular locationi

  • Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99Cytoplasmic
Transmembranei10 – 3223Helical; Name=1Add
BLAST
Topological domaini33 – 5826PeriplasmicAdd
BLAST
Transmembranei59 – 7921Helical; Name=2Add
BLAST
Topological domaini80 – 845Cytoplasmic
Transmembranei85 – 10521Helical; Name=3Add
BLAST
Topological domaini106 – 12823PeriplasmicAdd
BLAST
Transmembranei129 – 15022Helical; Name=4Add
BLAST
Topological domaini151 – 16212CytoplasmicAdd
BLAST
Transmembranei163 – 18321Helical; Name=5Add
BLAST
Topological domaini184 – 20017PeriplasmicAdd
BLAST
Transmembranei201 – 22121Helical; Name=6Add
BLAST
Topological domaini222 – 27655CytoplasmicAdd
BLAST
Transmembranei277 – 29923Helical; Name=7Add
BLAST
Topological domaini300 – 31213PeriplasmicAdd
BLAST
Transmembranei313 – 33422Helical; Name=8Add
BLAST
Topological domaini335 – 3439Cytoplasmic
Transmembranei344 – 36421Helical; Name=9Add
BLAST
Topological domaini365 – 3695Periplasmic
Transmembranei370 – 39021Helical; Name=10Add
BLAST
Topological domaini391 – 40717CytoplasmicAdd
BLAST
Transmembranei408 – 42821Helical; Name=11Add
BLAST
Topological domaini429 – 44214PeriplasmicAdd
BLAST
Transmembranei443 – 46321Helical; Name=12Add
BLAST
Topological domaini464 – 49128CytoplasmicAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 241F → A: Decreases xylose transport. 1 Publication
Mutagenesisi83 – 831G → A: Abolishes xylose transport. 1 Publication
Mutagenesisi133 – 1331R → C, H or L: Abolishes xylose transport. 1 Publication
Mutagenesisi153 – 1531E → A: Abolishes xylose transport. 1 Publication
Mutagenesisi160 – 1601R → A: Abolishes xylose transport. 1 Publication
Mutagenesisi168 – 1681Q → A: Abolishes xylose transport. 1 Publication
Mutagenesisi288 – 2881Q → A: Abolishes xylose transport. 1 Publication
Mutagenesisi289 – 2891Q → A: Strongly decreases xylose transport. 1 Publication
Mutagenesisi294 – 2941N → A: Abolishes xylose transport. 1 Publication
Mutagenesisi298 – 2981Y → A: Abolishes xylose transport. 1 Publication
Mutagenesisi325 – 3251N → A: No effect on xylose transport. 1 Publication
Mutagenesisi340 – 3401G → A: Abolishes xylose transport. 1 Publication
Mutagenesisi341 – 3411R → A or W: Abolishes xylose transport. 1 Publication
Mutagenesisi392 – 3921W → A: Abolishes xylose transport. 1 Publication
Mutagenesisi397 – 3971E → A: Abolishes xylose transport. 1 Publication
Mutagenesisi404 – 4041R → A: Strongly decreases xylose transport. 1 Publication
Mutagenesisi415 – 4151Q → A: Strongly decreases xylose transport.
Mutagenesisi416 – 4161W → A: Strongly decreases xylose transport. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491D-xylose-proton symporterPRO_0000050294Add
BLAST

Proteomic databases

PaxDbiP0AGF4.
PRIDEiP0AGF4.

Expressioni

Inductioni

By xylose.

Interactioni

Protein-protein interaction databases

BioGridi4262660. 7 interactions.
STRINGi511145.b4031.

Structurei

Secondary structure

1
491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2923Combined sources
Helixi30 – 334Combined sources
Helixi35 – 428Combined sources
Helixi44 – 463Combined sources
Helixi50 – 6213Combined sources
Helixi64 – 8118Combined sources
Helixi84 – 10320Combined sources
Turni105 – 1095Combined sources
Beta strandi112 – 1176Combined sources
Helixi120 – 1245Combined sources
Helixi126 – 15227Combined sources
Helixi157 – 1593Combined sources
Helixi160 – 18627Combined sources
Beta strandi187 – 1893Combined sources
Turni191 – 1977Combined sources
Helixi198 – 2047Combined sources
Helixi207 – 21610Combined sources
Helixi217 – 2193Combined sources
Helixi224 – 2296Combined sources
Helixi233 – 26634Combined sources
Helixi269 – 2724Combined sources
Helixi277 – 29014Combined sources
Helixi293 – 30614Combined sources
Helixi311 – 33929Combined sources
Helixi342 – 36423Combined sources
Helixi369 – 38416Combined sources
Turni385 – 3884Combined sources
Helixi389 – 3979Combined sources
Turni401 – 4033Combined sources
Helixi404 – 42320Combined sources
Helixi425 – 4295Combined sources
Helixi431 – 4399Combined sources
Helixi443 – 46220Combined sources
Helixi471 – 4744Combined sources
Helixi475 – 4773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GBYX-ray2.81A1-491[»]
4GBZX-ray2.89A1-491[»]
4GC0X-ray2.60A1-491[»]
4JA3X-ray3.80A/B2-485[»]
4JA4X-ray4.20A/B/C2-485[»]
4QIQX-ray3.51A6-480[»]
ProteinModelPortaliP0AGF4.
SMRiP0AGF4. Positions 5-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni288 – 2947Monosaccharide binding

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107QNK. Bacteria.
ENOG410XNQK. LUCA.
HOGENOMiHOG000202868.
InParanoidiP0AGF4.
KOiK08138.
OMAiWTSNFAI.
PhylomeDBiP0AGF4.

Family and domain databases

CDDicd06174. MFS. 1 hit.
InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSiPR00171. SUGRTRNSPORT.
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00879. SP. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AGF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTQYNSSYI FSITLVATLG GLLFGYDTAV ISGTVESLNT VFVAPQNLSE
60 70 80 90 100
SAANSLLGFC VASALIGCII GGALGGYCSN RFGRRDSLKI AAVLFFISGV
110 120 130 140 150
GSAWPELGFT SINPDNTVPV YLAGYVPEFV IYRIIGGIGV GLASMLSPMY
160 170 180 190 200
IAELAPAHIR GKLVSFNQFA IIFGQLLVYC VNYFIARSGD ASWLNTDGWR
210 220 230 240 250
YMFASECIPA LLFLMLLYTV PESPRWLMSR GKQEQAEGIL RKIMGNTLAT
260 270 280 290 300
QAVQEIKHSL DHGRKTGGRL LMFGVGVIVI GVMLSIFQQF VGINVVLYYA
310 320 330 340 350
PEVFKTLGAS TDIALLQTII VGVINLTFTV LAIMTVDKFG RKPLQIIGAL
360 370 380 390 400
GMAIGMFSLG TAFYTQAPGI VALLSMLFYV AAFAMSWGPV CWVLLSEIFP
410 420 430 440 450
NAIRGKALAI AVAAQWLANY FVSWTFPMMD KNSWLVAHFH NGFSYWIYGC
460 470 480 490
MGVLAALFMW KFVPETKGKT LEELEALWEP ETKKTQQTAT L
Length:491
Mass (Da):53,608
Last modified:December 20, 2005 - v1
Checksum:i2AF1AF9756C0B722
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641A → V in CAA29863 (PubMed:2836810).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02812 Genomic DNA. Translation: AAA79016.1.
U00006 Genomic DNA. Translation: AAC43125.1.
U00096 Genomic DNA. Translation: AAC77001.1.
AP009048 Genomic DNA. Translation: BAE78033.1.
X06663 Genomic DNA. Translation: CAA29863.1.
PIRiA26430.
RefSeqiNP_418455.1. NC_000913.3.
WP_001097274.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77001; AAC77001; b4031.
BAE78033; BAE78033; BAE78033.
GeneIDi948529.
KEGGiecj:JW3991.
eco:b4031.
PATRICi32123595. VBIEscCol129921_4146.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02812 Genomic DNA. Translation: AAA79016.1.
U00006 Genomic DNA. Translation: AAC43125.1.
U00096 Genomic DNA. Translation: AAC77001.1.
AP009048 Genomic DNA. Translation: BAE78033.1.
X06663 Genomic DNA. Translation: CAA29863.1.
PIRiA26430.
RefSeqiNP_418455.1. NC_000913.3.
WP_001097274.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GBYX-ray2.81A1-491[»]
4GBZX-ray2.89A1-491[»]
4GC0X-ray2.60A1-491[»]
4JA3X-ray3.80A/B2-485[»]
4JA4X-ray4.20A/B/C2-485[»]
4QIQX-ray3.51A6-480[»]
ProteinModelPortaliP0AGF4.
SMRiP0AGF4. Positions 5-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262660. 7 interactions.
STRINGi511145.b4031.

Protein family/group databases

TCDBi2.A.1.1.3. the major facilitator superfamily (mfs).

Proteomic databases

PaxDbiP0AGF4.
PRIDEiP0AGF4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77001; AAC77001; b4031.
BAE78033; BAE78033; BAE78033.
GeneIDi948529.
KEGGiecj:JW3991.
eco:b4031.
PATRICi32123595. VBIEscCol129921_4146.

Organism-specific databases

EchoBASEiEB1069.
EcoGeneiEG11076. xylE.

Phylogenomic databases

eggNOGiENOG4107QNK. Bacteria.
ENOG410XNQK. LUCA.
HOGENOMiHOG000202868.
InParanoidiP0AGF4.
KOiK08138.
OMAiWTSNFAI.
PhylomeDBiP0AGF4.

Enzyme and pathway databases

BioCyciEcoCyc:XYLE-MONOMER.
ECOL316407:JW3991-MONOMER.
MetaCyc:XYLE-MONOMER.

Miscellaneous databases

PROiP0AGF4.

Family and domain databases

CDDicd06174. MFS. 1 hit.
InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
PRINTSiPR00171. SUGRTRNSPORT.
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00879. SP. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYLE_ECOLI
AccessioniPrimary (citable) accession number: P0AGF4
Secondary accession number(s): P09098, Q2M6S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: September 7, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

E.coli has two D-xylose transport systems that accumulate sugar against a concentration gradient: the XylE system which utilizes the electrochemical gradient of protons and that is insensitive to cold osmotic shock and the XylF system that uses a high-energy phosphate compound and is sensitive to cold osmotic shock.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.