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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)DescriptionActionsGraphical viewLength
Binding sitei168Monosaccharide1
Binding sitei392Monosaccharide1
Binding sitei415Monosaccharide1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Topological domaini1 – 9Cytoplasmic9
Transmembranei10 – 32Helical; Name=1Add BLAST23
Topological domaini33 – 58PeriplasmicAdd BLAST26
Transmembranei59 – 79Helical; Name=2Add BLAST21
Topological domaini80 – 84Cytoplasmic5
Transmembranei85 – 105Helical; Name=3Add BLAST21
Topological domaini106 – 128PeriplasmicAdd BLAST23
Transmembranei129 – 150Helical; Name=4Add BLAST22
Topological domaini151 – 162CytoplasmicAdd BLAST12
Transmembranei163 – 183Helical; Name=5Add BLAST21
Topological domaini184 – 200PeriplasmicAdd BLAST17
Transmembranei201 – 221Helical; Name=6Add BLAST21
Topological domaini222 – 276CytoplasmicAdd BLAST55
Transmembranei277 – 299Helical; Name=7Add BLAST23
Topological domaini300 – 312PeriplasmicAdd BLAST13
Transmembranei313 – 334Helical; Name=8Add BLAST22
Topological domaini335 – 343Cytoplasmic9
Transmembranei344 – 364Helical; Name=9Add BLAST21
Topological domaini365 – 369Periplasmic5
Transmembranei370 – 390Helical; Name=10Add BLAST21
Topological domaini391 – 407CytoplasmicAdd BLAST17
Transmembranei408 – 428Helical; Name=11Add BLAST21
Topological domaini429 – 442PeriplasmicAdd BLAST14
Transmembranei443 – 463Helical; Name=12Add BLAST21
Topological domaini464 – 491CytoplasmicAdd BLAST28

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)DescriptionActionsGraphical viewLength
Mutagenesisi24F → A: Decreases xylose transport. 1 Publication1
Mutagenesisi83G → A: Abolishes xylose transport. 1 Publication1
Mutagenesisi133R → C, H or L: Abolishes xylose transport. 1 Publication1
Mutagenesisi153E → A: Abolishes xylose transport. 1 Publication1
Mutagenesisi160R → A: Abolishes xylose transport. 1 Publication1
Mutagenesisi168Q → A: Abolishes xylose transport. 1 Publication1
Mutagenesisi288Q → A: Abolishes xylose transport. 1 Publication1
Mutagenesisi289Q → A: Strongly decreases xylose transport. 1 Publication1
Mutagenesisi294N → A: Abolishes xylose transport. 1 Publication1
Mutagenesisi298Y → A: Abolishes xylose transport. 1 Publication1
Mutagenesisi325N → A: No effect on xylose transport. 1 Publication1
Mutagenesisi340G → A: Abolishes xylose transport. 1 Publication1
Mutagenesisi341R → A or W: Abolishes xylose transport. 1 Publication1
Mutagenesisi392W → A: Abolishes xylose transport. 1 Publication1
Mutagenesisi397E → A: Abolishes xylose transport. 1 Publication1
Mutagenesisi404R → A: Strongly decreases xylose transport. 1 Publication1
Mutagenesisi415Q → A: Strongly decreases xylose transport. 1
Mutagenesisi416W → A: Strongly decreases xylose transport. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000502941 – 491D-xylose-proton symporterAdd BLAST491

Proteomic databases

PaxDbiP0AGF4.
PRIDEiP0AGF4.

Expressioni

Inductioni

By xylose.

Interactioni

Protein-protein interaction databases

BioGridi4262660. 7 interactors.
STRINGi511145.b4031.

Structurei

Secondary structure

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 29Combined sources23
Helixi30 – 33Combined sources4
Helixi35 – 42Combined sources8
Helixi44 – 46Combined sources3
Helixi50 – 62Combined sources13
Helixi64 – 81Combined sources18
Helixi84 – 103Combined sources20
Turni105 – 109Combined sources5
Beta strandi112 – 117Combined sources6
Helixi120 – 124Combined sources5
Helixi126 – 152Combined sources27
Helixi157 – 159Combined sources3
Helixi160 – 186Combined sources27
Beta strandi187 – 189Combined sources3
Turni191 – 197Combined sources7
Helixi198 – 204Combined sources7
Helixi207 – 216Combined sources10
Helixi217 – 219Combined sources3
Helixi224 – 229Combined sources6
Helixi233 – 266Combined sources34
Helixi269 – 272Combined sources4
Helixi277 – 290Combined sources14
Helixi293 – 306Combined sources14
Helixi311 – 339Combined sources29
Helixi342 – 364Combined sources23
Helixi369 – 384Combined sources16
Turni385 – 388Combined sources4
Helixi389 – 397Combined sources9
Turni401 – 403Combined sources3
Helixi404 – 423Combined sources20
Helixi425 – 429Combined sources5
Helixi431 – 439Combined sources9
Helixi443 – 462Combined sources20
Helixi471 – 474Combined sources4
Helixi475 – 477Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni288 – 294Monosaccharide binding7

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)DescriptionActionsGraphical viewLength
Sequence conflicti64A → V in CAA29863 (PubMed:2836810).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262660. 7 interactors.
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: November 30, 2016
This is version 93 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.