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Protein

Lipid A biosynthesis lauroyltransferase

Gene

lpxL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of laurate from lauroyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(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 Kdo(2)-(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 Kdo(2)-lipid IV(A)1 Publication
  1. Vmax=95 µmol/min/mg enzyme toward lauroyl-ACP1 Publication
  2. Vmax=221 µmol/min/mg enzyme toward Kdo(2)-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

  • lauroyltransferase activity Source: UniProtKB-HAMAP
  • transferase activity Source: EcoCyc

GO - Biological processi

  • Kdo2-lipid A biosynthetic process Source: UniProtKB-HAMAP
  • lipid A biosynthetic process Source: EcoliWiki
  • lipopolysaccharide biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:LAUROYLACYLTRAN-MONOMER.
ECOL316407:JW1041-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

  • Cell inner membrane UniRule annotation3 Publications; Single-pass membrane protein UniRule annotation

Topology

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

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB-HAMAP
  • membrane Source: EcoliWiki
  • plasma membrane Source: EcoCyc
Complete GO annotation...

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. 69 interactors.
IntActiP0ACV0. 9 interactors.
STRINGi511145.b1054.

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.
InterProiIPR004960. LipA_acyltrans.
IPR011920. Lipid_A_LpxL_LpxP.
[Graphical view]
PfamiPF03279. Lip_A_acyltrans. 1 hit.
[Graphical view]
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.
PATRICi32117345. VBIEscCol129921_1095.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP0ACV0.
SMRiP0ACV0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262842. 69 interactors.
IntActiP0ACV0. 9 interactors.
STRINGi511145.b1054.

Proteomic databases

PaxDbiP0ACV0.
PRIDEiP0ACV0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74138; AAC74138; b1054.
BAA35852; BAA35852; BAA35852.
GeneIDi946216.
KEGGiecj:JW1041.
eco:b1054.
PATRICi32117345. VBIEscCol129921_1095.

Organism-specific databases

EchoBASEiEB0459.
EcoGeneiEG10464. lpxL.

Phylogenomic databases

eggNOGiENOG4105D1S. Bacteria.
COG1560. LUCA.
HOGENOMiHOG000265960.
InParanoidiP0ACV0.
KOiK02517.
OMAiILCLPYP.
PhylomeDBiP0ACV0.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00360; UER00485.
BioCyciEcoCyc:LAUROYLACYLTRAN-MONOMER.
ECOL316407:JW1041-MONOMER.
MetaCyc:LAUROYLACYLTRAN-MONOMER.
BRENDAi2.3.1.B29. 2026.

Miscellaneous databases

PROiP0ACV0.

Family and domain databases

CDDicd07984. LPLAT_LABLAT-like. 1 hit.
HAMAPiMF_01942. Lipid_A_LpxL_LpxP. 1 hit.
InterProiIPR004960. LipA_acyltrans.
IPR011920. Lipid_A_LpxL_LpxP.
[Graphical view]
PfamiPF03279. Lip_A_acyltrans. 1 hit.
[Graphical view]
PIRSFiPIRSF026649. MsbB. 1 hit.
TIGRFAMsiTIGR02207. lipid_A_htrB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLPXL_ECOLI
AccessioniPrimary (citable) accession number: P0ACV0
Secondary accession number(s): P24187
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: November 2, 2016
This is version 91 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, 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.