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Protein

Lipid-A-disaccharide synthase

Gene

lpxB

Organism
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.UniRule annotation

Catalytic activityi

UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + 2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate = UDP + 2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate.UniRule annotation

Pathway:ilipid IV(A) biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (lpxA)
  2. UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase (lpxC)
  3. UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (lpxD)
  4. UDP-2,3-diacylglucosamine hydrolase (lpxH)
  5. Lipid-A-disaccharide synthase (lpxB)
  6. Tetraacyldisaccharide 4'-kinase (lpxK)
This subpathway is part of the pathway lipid IV(A) biosynthesis, which is itself part of Glycolipid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine, the pathway lipid IV(A) biosynthesis and in Glycolipid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00359; UER00481.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipid-A-disaccharide synthaseUniRule annotation (EC:2.4.1.182UniRule annotation)
Gene namesi
Name:lpxBUniRule annotation
Ordered Locus Names:ECUMN_0179
OrganismiEscherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Taxonomic identifieri585056 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000007097 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Lipid-A-disaccharide synthasePRO_1000191480Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB7N849.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LpxB family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0763.
HOGENOMiHOG000018003.
KOiK00748.
OMAiTVHFVCP.
OrthoDBiEOG6FBWZR.

Family and domain databases

HAMAPiMF_00392. LpxB.
InterProiIPR003835. Glyco_trans_19.
[Graphical view]
PfamiPF02684. LpxB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00215. lpxB. 1 hit.

Sequencei

Sequence statusi: Complete.

B7N849-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEQRPLTIA LVAGETSGDI LGAGLIRALK ERVPNARFVG VAGPRMQAEG
60 70 80 90 100
CEAWYEMEEL AVMGIVEVLG RLRRLLHIRA DLTTRFGELK PDVFVGIDAP
110 120 130 140 150
DFNITLEGNL KKQGIKTIHY VSPSVWAWRQ KRVFKIGRAT DLVLAFLPFE
160 170 180 190 200
KAFYDKYNVP CRFIGHTMAD AMPLDPDKNG ARDVLGIPHD AHCLALLPGS
210 220 230 240 250
RGAEVEMLSA DFLKTAQLLR QTYPDLEIVV PLVNAKRREQ FERIKAEVAP
260 270 280 290 300
DLSVHMLDGL GREAMVASDA ALLASGTAAL ECMLAKCPMV VGYRMKPFTF
310 320 330 340 350
WLAKRLVKTD YVSLPNLLAG RELVKELLQE ECEPQKLAAA LLPLLANGKT
360 370 380
SHAMHDTFRE LHQQIRCNAD EQAAQAVLEL AQ
Length:382
Mass (Da):42,360
Last modified:February 10, 2009 - v1
Checksum:i2D9A8398E241BC16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928163 Genomic DNA. Translation: CAR11399.1.
RefSeqiWP_000139685.1. NC_011751.1.
YP_002410955.1. NC_011751.1.

Genome annotation databases

EnsemblBacteriaiCAR11399; CAR11399; ECUMN_0179.
GeneIDi7157009.
KEGGieum:ECUMN_0179.
PATRICi18439558. VBIEscCol32010_0373.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928163 Genomic DNA. Translation: CAR11399.1.
RefSeqiWP_000139685.1. NC_011751.1.
YP_002410955.1. NC_011751.1.

3D structure databases

ProteinModelPortaliB7N849.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAR11399; CAR11399; ECUMN_0179.
GeneIDi7157009.
KEGGieum:ECUMN_0179.
PATRICi18439558. VBIEscCol32010_0373.

Phylogenomic databases

eggNOGiCOG0763.
HOGENOMiHOG000018003.
KOiK00748.
OMAiTVHFVCP.
OrthoDBiEOG6FBWZR.

Enzyme and pathway databases

UniPathwayiUPA00359; UER00481.

Family and domain databases

HAMAPiMF_00392. LpxB.
InterProiIPR003835. Glyco_trans_19.
[Graphical view]
PfamiPF02684. LpxB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00215. lpxB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UMN026 / ExPEC.

Entry informationi

Entry nameiLPXB_ECOLU
AccessioniPrimary (citable) accession number: B7N849
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: July 22, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.