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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei17 – 3721HelicalUniRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi132 – 1321H → A: Almost loss of activity. 1 Publication
Mutagenesisi137 – 1371E → A: Almost loss of activity. 1 Publication
Mutagenesisi169 – 1691R → A: 169-fold decrease in activity. 1 Publication
Mutagenesisi200 – 2001D → A: 14-fold decrease in activity. 1 Publication
Mutagenesisi238 – 2381P → A: Slight decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306Lipid A biosynthesis lauroyltransferasePRO_0000201774Add
BLAST

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 interactions.
IntActiP0ACV0. 9 interactions.
STRINGi511145.b1054.

Structurei

3D structure databases

ProteinModelPortaliP0ACV0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi132 – 1376HXXXXD motifUniRule annotation1 Publication

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.
OrthoDBiEOG657J8B.
PhylomeDBiP0ACV0.

Family and domain databases

HAMAPiMF_01942. Lipid_A_LpxL_LpxP.
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262842. 69 interactions.
IntActiP0ACV0. 9 interactions.
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.
OrthoDBiEOG657J8B.
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

HAMAPiMF_01942. Lipid_A_LpxL_LpxP.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing, mutational analysis, and transcriptional regulation of the Escherichia coli htrB gene."
    Karow M.L., Georgopoulos C.
    Mol. Microbiol. 5:2285-2292(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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.
  5. "Multicopy suppression: an approach to understanding intracellular functioning of the protein export system."
    Ueguchi C., Ito K.
    J. Bacteriol. 174:1454-1461(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-306.
    Strain: K12.
  6. "Biosynthesis of lipid A in Escherichia coli. Acyl carrier protein-dependent incorporation of laurate and myristate."
    Brozek K.A., Raetz C.R.H.
    J. Biol. Chem. 265:15410-15417(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY.
  7. "Isolation and characterization of the Escherichia coli htrB gene, whose product is essential for bacterial viability above 33 degrees C in rich media."
    Karow M., Fayet O., Cegielska A., Ziegelhoffer T., Georgopoulos C.
    J. Bacteriol. 173:741-750(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  8. "Function of the htrB high temperature requirement gene of Escherchia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate."
    Clementz T., Bednarski J.J., Raetz C.R.
    J. Biol. Chem. 271:12095-12102(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY, SUBCELLULAR LOCATION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis."
    Six D.A., Carty S.M., Guan Z., Raetz C.R.
    Biochemistry 47:8623-8637(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-132; GLU-137; ARG-169; ASP-200 AND PRO-238.

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: January 20, 2016
This is version 88 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.