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Protein

Lipopolysaccharide 1,2-glucosyltransferase

Gene

rfaJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Adds the glucose(II) group on the galactose(I) group of LPS.By similarity

Catalytic activityi

UDP-glucose + [lipopolysaccharide] = UDP + D-glucosyl-[lipopolysaccharide].

Pathwayi: LPS core biosynthesis

This protein is involved in the pathway LPS core biosynthesis, which is part of Bacterial outer membrane biogenesis.
View all proteins of this organism that are known to be involved in the pathway LPS core biosynthesis and in Bacterial outer membrane biogenesis.

GO - Molecular functioni

GO - Biological processi

  • lipopolysaccharide core region biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG11353-MONOMER.
ECOL316407:JW3601-MONOMER.
MetaCyc:EG11353-MONOMER.
UniPathwayiUPA00958.

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipopolysaccharide 1,2-glucosyltransferase (EC:2.4.1.58)
Gene namesi
Name:rfaJ
Synonyms:waaJ
Ordered Locus Names:b3626, JW3601
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11353. rfaJ.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Lipopolysaccharide 1,2-glucosyltransferasePRO_0000206066Add
BLAST

Proteomic databases

PaxDbiP27129.

Interactioni

Protein-protein interaction databases

BioGridi4261893. 194 interactions.
DIPiDIP-10671N.
IntActiP27129. 6 interactions.
MINTiMINT-1248317.
STRINGi511145.b3626.

Structurei

3D structure databases

ProteinModelPortaliP27129.
SMRiP27129. Positions 34-274.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 8 family.Curated

Phylogenomic databases

eggNOGiENOG4105X1N. Bacteria.
COG1442. LUCA.
HOGENOMiHOG000126190.
InParanoidiP27129.
KOiK03276.
OMAiTVILHFC.
OrthoDBiEOG6X3W2K.
PhylomeDBiP27129.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR013645. Glyco_transf_8N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
PF08437. Glyco_transf_8C. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P27129-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSFPAIEID KVKAWDFRLA NINTSECLNV AYGVDANYLD GVGVSITSIV
60 70 80 90 100
LNNRHINLDF YIIADVYNDG FFQKIAKLAE QNQLRITLYR INTDKLQCLP
110 120 130 140 150
CTQVWSRAMY FRLFAFQLLG LTLDRLLYLD ADVVCKGDIS QLLHLGLNGA
160 170 180 190 200
VAAVVKDVEP MQEKAVSRLS DPELLGQYFN SGVVYLDLKK WADAKLTEKA
210 220 230 240 250
LSILMSKDNV YKYPDQDVMN VLLKGMTLFL PREYNTIYTI KSELKDKTHQ
260 270 280 290 300
NYKKLITEST LLIHYTGATK PWHKWAIYPS VKYYKIALEN SPWKDDSPRD
310 320 330
AKSIIEFKKR YKHLLVQHHY ISGIIAGVCY LCRKYYRK
Length:338
Mass (Da):39,040
Last modified:October 1, 1994 - v2
Checksum:i819428EA13F1959A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti310 – 33829RYKHL…KYYRK → DINIF in AAA24087 (PubMed:1624461).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80599 Genomic DNA. Translation: AAA24087.1.
U00039 Genomic DNA. Translation: AAB18603.1.
U00096 Genomic DNA. Translation: AAC76650.1.
AP009048 Genomic DNA. Translation: BAE77666.1.
PIRiS47847.
RefSeqiNP_418083.1. NC_000913.3.
WP_000376841.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76650; AAC76650; b3626.
BAE77666; BAE77666; BAE77666.
GeneIDi948142.
KEGGiecj:JW3601.
eco:b3626.
PATRICi32122739. VBIEscCol129921_3746.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80599 Genomic DNA. Translation: AAA24087.1.
U00039 Genomic DNA. Translation: AAB18603.1.
U00096 Genomic DNA. Translation: AAC76650.1.
AP009048 Genomic DNA. Translation: BAE77666.1.
PIRiS47847.
RefSeqiNP_418083.1. NC_000913.3.
WP_000376841.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP27129.
SMRiP27129. Positions 34-274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261893. 194 interactions.
DIPiDIP-10671N.
IntActiP27129. 6 interactions.
MINTiMINT-1248317.
STRINGi511145.b3626.

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

Proteomic databases

PaxDbiP27129.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76650; AAC76650; b3626.
BAE77666; BAE77666; BAE77666.
GeneIDi948142.
KEGGiecj:JW3601.
eco:b3626.
PATRICi32122739. VBIEscCol129921_3746.

Organism-specific databases

EchoBASEiEB1328.
EcoGeneiEG11353. rfaJ.

Phylogenomic databases

eggNOGiENOG4105X1N. Bacteria.
COG1442. LUCA.
HOGENOMiHOG000126190.
InParanoidiP27129.
KOiK03276.
OMAiTVILHFC.
OrthoDBiEOG6X3W2K.
PhylomeDBiP27129.

Enzyme and pathway databases

UniPathwayiUPA00958.
BioCyciEcoCyc:EG11353-MONOMER.
ECOL316407:JW3601-MONOMER.
MetaCyc:EG11353-MONOMER.

Miscellaneous databases

PROiP27129.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR013645. Glyco_transf_8N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
PF08437. Glyco_transf_8C. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structures of the rfaB, rfaI, rfaJ, and rfaS genes of Escherichia coli K-12 and their roles in assembly of the lipopolysaccharide core."
    Pradel E., Parker C.T., Schnaitman C.A.
    J. Bacteriol. 174:4736-4745(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiRFAJ_ECOLI
AccessioniPrimary (citable) accession number: P27129
Secondary accession number(s): Q2M7U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1994
Last modified: February 17, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.