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Protein

Putative phosphotransferase enzyme IIA component YadI

Gene

yadI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei9Tele-phosphohistidine intermediatePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:AGAX-MONOMER
MetaCyc:AGAX-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Putative phosphotransferase enzyme IIA component YadI
Alternative name(s):
Putative PTS system EIIA component
Gene namesi
Name:yadI
Ordered Locus Names:b0129, JW0125
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12322 yadI

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001867081 – 146Putative phosphotransferase enzyme IIA component YadIAdd BLAST146

Proteomic databases

PaxDbiP36881
PRIDEiP36881

Interactioni

Protein-protein interaction databases

STRINGi316385.ECDH10B_0109

Structurei

3D structure databases

ProteinModelPortaliP36881
SMRiP36881
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 124PTS EIIA type-4PROSITE-ProRule annotationAdd BLAST124

Domaini

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.

Phylogenomic databases

eggNOGiENOG4108YTN Bacteria
COG2893 LUCA
HOGENOMiHOG000095324
InParanoidiP36881
OMAiGWVIACH
PhylomeDBiP36881

Family and domain databases

CDDicd00006 PTS_IIA_man, 1 hit
Gene3Di3.40.50.510, 1 hit
InterProiView protein in InterPro
IPR004701 PTS_EIIA_man-typ
IPR036662 PTS_EIIA_man-typ_sf
IPR033887 PTS_IIA_man
PfamiView protein in Pfam
PF03610 EIIA-man, 1 hit
SUPFAMiSSF53062 SSF53062, 1 hit
PROSITEiView protein in PROSITE
PS51096 PTS_EIIA_TYPE_4, 1 hit

Sequencei

Sequence statusi: Complete.

P36881-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGWVITCHD DRAQEILDAL EKKHGALLQC RAVNFWRGLS SNMLSRMMCD
60 70 80 90 100
ALHEADSGEG VIFLTDIAGA PPYRVASLLS HKHSRCEVIS GVTLPLIEQM
110 120 130 140
MACRETMTSS EFRERIVELG APEVSSLWHQ QQKNPPFVLK HNLYEY
Length:146
Mass (Da):16,540
Last modified:November 1, 1997 - v2
Checksum:i9534A95A41130CE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC73240.1
AP009048 Genomic DNA Translation: BAB96706.2
PIRiA64736
RefSeqiNP_414671.1, NC_000913.3
WP_000901987.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73240; AAC73240; b0129
BAB96706; BAB96706; BAB96706
GeneIDi947397
KEGGiecj:JW0125
eco:b0129
PATRICifig|1411691.4.peg.2153

Similar proteinsi

Entry informationi

Entry nameiYADI_ECOLI
AccessioniPrimary (citable) accession number: P36881
Secondary accession number(s): P75658
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 130 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health