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Protein

PTS system fructose-like EIIB component 3

Gene

frwD

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

Functioni

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane.By similarity1 Publication

Catalytic activityi

[Protein]-N(pi)-phospho-L-histidine + D-fructose(Side 1) = [protein]-L-histidine + D-fructose 1-phosphate(Side 2).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei10Phosphocysteine intermediateBy similarityCurated1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase
Biological processPhosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG11912-MONOMER

Protein family/group databases

TCDBi4.A.2.1.10 the pts fructose-mannitol (fru) family

Names & Taxonomyi

Protein namesi
Recommended name:
PTS system fructose-like EIIB component 3By similarity (EC:2.7.1.202By similarity)
Alternative name(s):
Fructose-like phosphotransferase enzyme IIB component 3By similarity
Gene namesi
Name:frwD
Synonyms:yijN
Ordered Locus Names:b3953, JW3925
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11912 frwD

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001865051 – 113PTS system fructose-like EIIB component 3Add BLAST113

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10Phosphocysteine; by EIIAPROSITE-ProRule annotation1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP32676
PRIDEiP32676

Interactioni

Protein-protein interaction databases

BioGridi4263010, 6 interactors
IntActiP32676, 2 interactors
STRINGi316385.ECDH10B_4141

Structurei

Secondary structure

1113
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Turni13 – 17Combined sources5
Helixi18 – 30Combined sources13
Beta strandi34 – 41Combined sources8
Beta strandi44 – 47Combined sources4
Helixi51 – 56Combined sources6
Beta strandi58 – 66Combined sources9
Helixi71 – 74Combined sources4
Beta strandi79 – 82Combined sources4
Helixi84 – 89Combined sources6
Helixi92 – 103Combined sources12
Beta strandi104 – 106Combined sources3
Beta strandi108 – 111Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4TN5X-ray2.29A/B1-113[»]
ProteinModelPortaliP32676
SMRiP32676
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 100PTS EIIB type-2PROSITE-ProRule annotationAdd BLAST100

Domaini

The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108XCZ Bacteria
COG1445 LUCA
HOGENOMiHOG000231313
KOiK11202
OMAiCISGVAH
PhylomeDBiP32676

Family and domain databases

CDDicd05569 PTS_IIB_fructose, 1 hit
InterProiView protein in InterPro
IPR036095 PTS_EIIB-like_sf
IPR013011 PTS_EIIB_2
IPR003501 PTS_EIIB_2/3
IPR003353 PTS_IIB_fruc
PfamiView protein in Pfam
PF02302 PTS_IIB, 1 hit
SUPFAMiSSF52794 SSF52794, 1 hit
TIGRFAMsiTIGR00829 FRU, 1 hit
PROSITEiView protein in PROSITE
PS51099 PTS_EIIB_TYPE_2, 1 hit

Sequencei

Sequence statusi: Complete.

P32676-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYLVAVTAC VSGVAHTYMA AERLEKLCLL EKWGVSIETQ GALGTENRLA
60 70 80 90 100
DEDIRRADVA LLITDIELAG AERFEHCRYV QCSIYAFLRE PQRVMSAVRK
110
VLSAPQQTHL ILE
Length:113
Mass (Da):12,637
Last modified:October 1, 1993 - v1
Checksum:i36252AB21DDB09EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA Translation: AAC43059.1
U00096 Genomic DNA Translation: AAC76935.1
AP009048 Genomic DNA Translation: BAE77358.1
PIRiD65202
RefSeqiNP_418388.1, NC_000913.3
WP_000323846.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76935; AAC76935; b3953
BAE77358; BAE77358; BAE77358
GeneIDi948452
KEGGiecj:JW3925
eco:b3953
PATRICifig|1411691.4.peg.2752

Similar proteinsi

Entry informationi

Entry nameiPTFB3_ECOLI
AccessioniPrimary (citable) accession number: P32676
Secondary accession number(s): Q2M8P8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: March 28, 2018
This is version 132 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health