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Protein

Lipid A biosynthesis lauroyltransferase

Gene

lpxL

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

Functioni

Catalyzes the transfer of laurate from lauroyl-acyl carrier protein (ACP) to Kdo2-lipid IV(A) to form Kdo2-(lauroyl)-lipid IV(A). Has 10 fold selectivity for lauroyl-ACP over myristoyl-ACP. In vitro, can also catalyze a slow second acylation reaction leading to the formation of Kdo2-(dilauroyl)-lipid IV(A).3 Publications

Catalytic activityi

A dodecanoyl-[acyl-carrier protein] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A) = (Kdo)2-(dodecanoyl)-lipid IV(A) + a holo-[acyl-carrier protein].UniRule annotation1 Publication

Kineticsi

  1. KM=7 µM for lauroyl-ACP1 Publication
  2. KM=15 µM for Kdo2-lipid IV(A)1 Publication
  1. Vmax=95 µmol/min/mg enzyme toward lauroyl-ACP1 Publication
  2. Vmax=221 µmol/min/mg enzyme toward Kdo2-lipid IV(A)1 Publication

Pathwayi: KDO(2)-lipid A biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A).UniRule annotation3 Publications
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 3-deoxy-D-manno-octulosonic acid transferase (waaA)
  2. 3-deoxy-D-manno-octulosonic acid transferase (waaA)
  3. Lipid A biosynthesis lauroyltransferase (lpxL)
  4. Lipid A biosynthesis myristoyltransferase (lpxM)
This subpathway is part of the pathway KDO(2)-lipid 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 KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A), the pathway KDO(2)-lipid A biosynthesis and in Glycolipid biosynthesis.

Pathwayi: lipopolysaccharide biosynthesis

This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation3 Publications
View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.

GO - Molecular functioni

  • transferase activity Source: EcoCyc
  • transferase activity, transferring acyl groups Source: UniProtKB-KW

GO - Biological processi

  • Kdo2-lipid A biosynthetic process Source: UniProtKB-UniPathway
  • lipid A biosynthetic process Source: EcoliWiki
  • lipopolysaccharide biosynthetic process Source: UniProtKB-UniPathway

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processLipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:LAUROYLACYLTRAN-MONOMER
MetaCyc:LAUROYLACYLTRAN-MONOMER
BRENDAi2.3.1.B29 2026
UniPathwayiUPA00030
UPA00360; UER00485

Names & Taxonomyi

Protein namesi
Recommended name:
Lipid A biosynthesis lauroyltransferase1 PublicationUniRule annotation (EC:2.3.1.241UniRule annotation1 Publication)
Alternative name(s):
Kdo(2)-lipid IV(A) lauroyltransferaseUniRule annotation
Gene namesi
Name:lpxL1 PublicationUniRule annotation
Synonyms:htrB1 Publication, waaM
Ordered Locus Names:b1054Imported, JW1041Imported
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10464 lpxL

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei17 – 37HelicalUniRule annotationAdd BLAST21

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: EcoliWiki
  • plasma membrane Source: EcoCyc

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Inactivation leads to bacterial death at temperatures above 33 degrees Celsius. Phenotype at nonpermissive temperatures includes an arrest of cell division followed by the formation of bulges or filaments.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi132H → A: Almost loss of activity. 1 Publication1
Mutagenesisi137E → A: Almost loss of activity. 1 Publication1
Mutagenesisi169R → A: 169-fold decrease in activity. 1 Publication1
Mutagenesisi200D → A: 14-fold decrease in activity. 1 Publication1
Mutagenesisi238P → A: Slight decrease in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002017741 – 306Lipid A biosynthesis lauroyltransferaseAdd BLAST306

Proteomic databases

PaxDbiP0ACV0
PRIDEiP0ACV0

Expressioni

Inductioni

Is expressed at all temperatures, but accumulation of htrB transcripts slightly declines with raising temperature. Thus, its expression is not induced by heat shock.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4262842, 71 interactors
IntActiP0ACV0, 9 interactors
STRINGi316385.ECDH10B_1125

Structurei

3D structure databases

ProteinModelPortaliP0ACV0
SMRiP0ACV0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi132 – 137HXXXXD motifUniRule annotation1 Publication6

Sequence similaritiesi

Belongs to the LpxL/LpxM/LpxP family.UniRule annotationCurated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D1S Bacteria
COG1560 LUCA
HOGENOMiHOG000265960
InParanoidiP0ACV0
KOiK02517
OMAiILCLPYP
PhylomeDBiP0ACV0

Family and domain databases

CDDicd07984 LPLAT_LABLAT-like, 1 hit
HAMAPiMF_01942 Lipid_A_LpxL_LpxP, 1 hit
InterProiView protein in InterPro
IPR004960 LipA_acyltrans
IPR011920 Lipid_A_LpxL_LpxP
PANTHERiPTHR30606 PTHR30606, 1 hit
PfamiView protein in Pfam
PF03279 Lip_A_acyltrans, 1 hit
PIRSFiPIRSF026649 MsbB, 1 hit
TIGRFAMsiTIGR02207 lipid_A_htrB, 1 hit

Sequencei

Sequence statusi: Complete.

P0ACV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNLPKFSTA LLHPRYWLTW LGIGVLWLVV QLPYPVIYRL GCGLGKLALR
60 70 80 90 100
FMKRRAKIVH RNLELCFPEM SEQERRKMVV KNFESVGMGL METGMAWFWP
110 120 130 140 150
DRRIARWTEV IGMEHIRDVQ AQKRGILLVG IHFLTLELGA RQFGMQEPGI
160 170 180 190 200
GVYRPNDNPL IDWLQTWGRL RSNKSMLDRK DLKGMIKALK KGEVVWYAPD
210 220 230 240 250
HDYGPRSSVF VPLFAVEQAA TTTGTWMLAR MSGACLVPFV PRRKPDGKGY
260 270 280 290 300
QLIMLPPECS PPLDDAETTA AWMNKVVEKC IMMAPEQYMW LHRRFKTRPE

GVPSRY
Length:306
Mass (Da):35,407
Last modified:November 22, 2005 - v1
Checksum:iAEA70A5EB10653B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61000 Genomic DNA Translation: CAA43317.1
U00096 Genomic DNA Translation: AAC74138.1
AP009048 Genomic DNA Translation: BAA35852.1
X59939 Genomic DNA No translation available.
PIRiS16888
RefSeqiNP_415572.1, NC_000913.3
WP_000183364.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74138; AAC74138; b1054
BAA35852; BAA35852; BAA35852
GeneIDi946216
KEGGiecj:JW1041
eco:b1054
PATRICifig|511145.12.peg.1095

Entry informationi

Entry nameiLPXL_ECOLI
AccessioniPrimary (citable) accession number: P0ACV0
Secondary accession number(s): P24187
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: March 28, 2018
This is version 98 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

Complete proteome, Reference proteome

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