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Protein

D-xylose-binding periplasmic protein

Gene

xylF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the high-affinity D-xylose membrane transport system. Binds with high affinity to xylose.

GO - Molecular functioni

  • monosaccharide binding Source: EcoCyc

GO - Biological processi

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

Keywords - Biological processi

Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:XYLF-MONOMER.
ECOL316407:JW3538-MONOMER.
MetaCyc:XYLF-MONOMER.

Protein family/group databases

TCDBi3.A.1.2.4. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
D-xylose-binding periplasmic protein
Gene namesi
Name:xylF
Synonyms:xylT
Ordered Locus Names:b3566, JW3538
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG20252. xylF.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 233 PublicationsAdd BLAST23
ChainiPRO_000003173824 – 330D-xylose-binding periplasmic proteinAdd BLAST307

Proteomic databases

EPDiP37387.
PaxDbiP37387.
PRIDEiP37387.

Interactioni

Protein-protein interaction databases

BioGridi4262541. 7 interactors.
IntActiP37387. 4 interactors.
STRINGi511145.b3566.

Structurei

Secondary structure

1330
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 33Combined sources7
Beta strandi36 – 38Combined sources3
Helixi41 – 53Combined sources13
Beta strandi57 – 62Combined sources6
Helixi67 – 79Combined sources13
Beta strandi83 – 88Combined sources6
Helixi96 – 103Combined sources8
Turni104 – 106Combined sources3
Beta strandi108 – 114Combined sources7
Beta strandi122 – 127Combined sources6
Helixi129 – 143Combined sources15
Beta strandi145 – 154Combined sources10
Helixi159 – 177Combined sources19
Beta strandi180 – 188Combined sources9
Helixi190 – 192Combined sources3
Helixi194 – 207Combined sources14
Turni208 – 210Combined sources3
Beta strandi214 – 219Combined sources6
Helixi220 – 231Combined sources12
Turni232 – 234Combined sources3
Turni236 – 238Combined sources3
Beta strandi239 – 241Combined sources3
Helixi248 – 256Combined sources9
Beta strandi262 – 264Combined sources3
Helixi267 – 282Combined sources16
Beta strandi290 – 294Combined sources5
Beta strandi296 – 305Combined sources10
Beta strandi308 – 310Combined sources3
Turni312 – 315Combined sources4
Helixi316 – 320Combined sources5
Turni321 – 323Combined sources3
Helixi327 – 329Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3M9WX-ray2.15A24-330[»]
3M9XX-ray2.20A24-330[»]
3MA0X-ray2.20A/B/C24-330[»]
ProteinModelPortaliP37387.
SMRiP37387.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37387.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105DFW. Bacteria.
COG4213. LUCA.
HOGENOMiHOG000240882.
InParanoidiP37387.
KOiK10543.
OMAiQQWVPEW.
PhylomeDBiP37387.

Family and domain databases

InterProiIPR028082. Peripla_BP_I.
IPR025997. SBP_2_dom.
IPR013456. XylF.
[Graphical view]
PfamiPF13407. Peripla_BP_4. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
TIGRFAMsiTIGR02634. xylF. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIKNILLTL CTSLLLTNVA AHAKEVKIGM AIDDLRLERW QKDRDIFVKK
60 70 80 90 100
AESLGAKVFV QSANGNEETQ MSQIENMINR GVDVLVIIPY NGQVLSNVVK
110 120 130 140 150
EAKQEGIKVL AYDRMINDAD IDFYISFDNE KVGELQAKAL VDIVPQGNYF
160 170 180 190 200
LMGGSPVDNN AKLFRAGQMK VLKPYVDSGK IKVVGDQWVD GWLPENALKI
210 220 230 240 250
MENALTANNN KIDAVVASND ATAGGAIQAL SAQGLSGKVA ISGQDADLAG
260 270 280 290 300
IKRIAAGTQT MTVYKPITLL ANTAAEIAVE LGNGQEPKAD TTLNNGLKDV
310 320 330
PSRLLTPIDV NKNNIKDTVI KDGFHKESEL
Length:330
Mass (Da):35,734
Last modified:October 1, 1994 - v1
Checksum:iE0AFC0326511B056
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18543.1.
U00096 Genomic DNA. Translation: AAC76590.1.
AP009048 Genomic DNA. Translation: BAE77727.1.
PIRiS47787.
RefSeqiNP_418023.1. NC_000913.3.
WP_000694881.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76590; AAC76590; b3566.
BAE77727; BAE77727; BAE77727.
GeneIDi948090.
KEGGiecj:JW3538.
eco:b3566.
PATRICi32122608. VBIEscCol129921_3681.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18543.1.
U00096 Genomic DNA. Translation: AAC76590.1.
AP009048 Genomic DNA. Translation: BAE77727.1.
PIRiS47787.
RefSeqiNP_418023.1. NC_000913.3.
WP_000694881.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3M9WX-ray2.15A24-330[»]
3M9XX-ray2.20A24-330[»]
3MA0X-ray2.20A/B/C24-330[»]
ProteinModelPortaliP37387.
SMRiP37387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262541. 7 interactors.
IntActiP37387. 4 interactors.
STRINGi511145.b3566.

Protein family/group databases

TCDBi3.A.1.2.4. the atp-binding cassette (abc) superfamily.

Proteomic databases

EPDiP37387.
PaxDbiP37387.
PRIDEiP37387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76590; AAC76590; b3566.
BAE77727; BAE77727; BAE77727.
GeneIDi948090.
KEGGiecj:JW3538.
eco:b3566.
PATRICi32122608. VBIEscCol129921_3681.

Organism-specific databases

EchoBASEiEB4153.
EcoGeneiEG20252. xylF.

Phylogenomic databases

eggNOGiENOG4105DFW. Bacteria.
COG4213. LUCA.
HOGENOMiHOG000240882.
InParanoidiP37387.
KOiK10543.
OMAiQQWVPEW.
PhylomeDBiP37387.

Enzyme and pathway databases

BioCyciEcoCyc:XYLF-MONOMER.
ECOL316407:JW3538-MONOMER.
MetaCyc:XYLF-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP37387.
PROiP37387.

Family and domain databases

InterProiIPR028082. Peripla_BP_I.
IPR025997. SBP_2_dom.
IPR013456. XylF.
[Graphical view]
PfamiPF13407. Peripla_BP_4. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
TIGRFAMsiTIGR02634. xylF. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiXYLF_ECOLI
AccessioniPrimary (citable) accession number: P37387
Secondary accession number(s): Q2M7M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 30, 2016
This is version 127 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, Direct protein sequencing, 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.