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Protein

Lipid A biosynthesis palmitoleoyltransferase

Gene

lpxP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of palmitoleate from palmitoleoyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(palmitoleoyl)-lipid IV(A). Required for the biosynthesis of a distinct molecular species of lipid A, which is present only in cells grown at low temperatures. It may confer a selective advantage to cells growing at lower temperatures by making the outer membrane a more effective barrier to harmful chemicals.2 Publications

Catalytic activityi

A (9Z)-hexadecenoyl-[acyl-carrier protein] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A) = (Kdo)(2)-((9Z)-hexadecenoyl)-lipid IV(A) + a holo-[acyl-carrier protein].UniRule annotation1 Publication

Pathwayi: lipopolysaccharide biosynthesis

This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation1 Publication
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

GO - Biological processi

  • Kdo2-lipid A biosynthetic process Source: EcoCyc
  • lipid A biosynthetic process Source: InterPro
  • lipopolysaccharide biosynthetic process Source: UniProtKB-UniPathway
  • response to cold Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipopolysaccharide biosynthesis, Stress response

Enzyme and pathway databases

BioCyciEcoCyc:PALMITOTRANS-MONOMER.
ECOL316407:JW2375-MONOMER.
MetaCyc:PALMITOTRANS-MONOMER.
BRENDAi2.3.1.B30. 2026.
UniPathwayiUPA00030.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipid A biosynthesis palmitoleoyltransferase1 PublicationUniRule annotation (EC:2.3.1.242UniRule annotation1 Publication)
Alternative name(s):
Kdo(2)-lipid IV(A) palmitoleoyltransferaseUniRule annotation
Gene namesi
Name:lpxP1 PublicationUniRule annotation
Synonyms:ddg
Ordered Locus Names:b2378, JW2375
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12901. lpxP.

Subcellular locationi

  • Cell inner membrane UniRule annotationCurated; Single-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei20 – 4021HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Disruption does not confer any obvious growth phenotype in nutrient broth at low temperatures, but mutant shows a 10-fold increase in sensitivity to rifampicin and vancomycin at 12 degrees Celsius compared with wild type cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306Lipid A biosynthesis palmitoleoyltransferasePRO_0000201781Add
BLAST

Proteomic databases

PaxDbiP0ACV2.
PRIDEiP0ACV2.

Expressioni

Inductioni

Induced more than 30-fold upon cold shock. The induced activity is maximal after 2 h of cold shock, and then gradually declines but does not disappear (PubMed:10092655). Induced in persister cells (PubMed:16768798).2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4260930. 142 interactions.
IntActiP0ACV2. 6 interactions.
STRINGi511145.b2378.

Structurei

3D structure databases

ProteinModelPortaliP0ACV2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D1S. Bacteria.
COG1560. LUCA.
HOGENOMiHOG000265960.
InParanoidiP0ACV2.
KOiK12974.
OMAiIGIHFMS.
OrthoDBiEOG657J8B.
PhylomeDBiP0ACV2.

Family and domain databases

HAMAPiMF_01942. Lipid_A_LpxL_LpxP.
MF_01943. Lipid_A_LpxP.
InterProiIPR004960. LipA_acyltrans.
IPR011920. Lipid_A_LpxL_LpxP.
IPR030857. Lipid_A_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.

P0ACV2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPQCKFSRE FLHPRYWLTW FGLGVLWLWV QLPYPVLCFL GTRIGAMARP
60 70 80 90 100
FLKRRESIAR KNLELCFPQH SAEEREKMIA ENFRSLGMAL VETGMAWFWP
110 120 130 140 150
DSRVRKWFDV EGLDNLKRAQ MQNRGVMVVG VHFMSLELGG RVMGLCQPMM
160 170 180 190 200
ATYRPHNNQL MEWVQTRGRM RSNKAMIGRN NLRGIVGALK KGEAVWFAPD
210 220 230 240 250
QDYGRKGSSF APFFAVENVA TTNGTYVLSR LSGAAMLTVT MVRKADYSGY
260 270 280 290 300
RLFITPEMEG YPTDENQAAA YMNKIIEKEI MRAPEQYLWI HRRFKTRPVG

ESSLYI
Length:306
Mass (Da):35,493
Last modified:November 22, 2005 - v1
Checksum:i58327F3D96C9E7B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49787 Genomic DNA. Translation: AAB66658.1.
U00096 Genomic DNA. Translation: AAC75437.2.
AP009048 Genomic DNA. Translation: BAA16248.1.
RefSeqiNP_416879.4. NC_000913.3.
WP_000484404.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75437; AAC75437; b2378.
BAA16248; BAA16248; BAA16248.
GeneIDi946847.
KEGGiecj:JW2375.
eco:b2378.
PATRICi32120133. VBIEscCol129921_2475.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49787 Genomic DNA. Translation: AAB66658.1.
U00096 Genomic DNA. Translation: AAC75437.2.
AP009048 Genomic DNA. Translation: BAA16248.1.
RefSeqiNP_416879.4. NC_000913.3.
WP_000484404.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0ACV2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260930. 142 interactions.
IntActiP0ACV2. 6 interactions.
STRINGi511145.b2378.

Proteomic databases

PaxDbiP0ACV2.
PRIDEiP0ACV2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75437; AAC75437; b2378.
BAA16248; BAA16248; BAA16248.
GeneIDi946847.
KEGGiecj:JW2375.
eco:b2378.
PATRICi32120133. VBIEscCol129921_2475.

Organism-specific databases

EchoBASEiEB2738.
EcoGeneiEG12901. lpxP.

Phylogenomic databases

eggNOGiENOG4105D1S. Bacteria.
COG1560. LUCA.
HOGENOMiHOG000265960.
InParanoidiP0ACV2.
KOiK12974.
OMAiIGIHFMS.
OrthoDBiEOG657J8B.
PhylomeDBiP0ACV2.

Enzyme and pathway databases

UniPathwayiUPA00030.
BioCyciEcoCyc:PALMITOTRANS-MONOMER.
ECOL316407:JW2375-MONOMER.
MetaCyc:PALMITOTRANS-MONOMER.
BRENDAi2.3.1.B30. 2026.

Miscellaneous databases

PROiP0ACV2.

Family and domain databases

HAMAPiMF_01942. Lipid_A_LpxL_LpxP.
MF_01943. Lipid_A_LpxP.
InterProiIPR004960. LipA_acyltrans.
IPR011920. Lipid_A_LpxL_LpxP.
IPR030857. Lipid_A_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. Sreekumar K.R., Schaechter M.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    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. "Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction at 12 degrees C of an acyltransferase specific for palmitoleoyl-acyl carrier protein."
    Carty S.M., Sreekumar K.R., Raetz C.R.
    J. Biol. Chem. 274:9677-9685(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INDUCTION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "An Escherichia coli mutant lacking the cold shock-induced palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated acyl chains and antibiotic hypersensitivity at 12 degrees C."
    Vorachek-Warren M.K., Carty S.M., Lin S., Cotter R.J., Raetz C.R.
    J. Biol. Chem. 277:14186-14193(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Persisters: a distinct physiological state of E. coli."
    Shah D., Zhang Z., Khodursky A., Kaldalu N., Kurg K., Lewis K.
    BMC Microbiol. 6:53-53(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION IN PERSISTER CELLS.
    Strain: K12.

Entry informationi

Entry nameiLPXP_ECOLI
AccessioniPrimary (citable) accession number: P0ACV2
Secondary accession number(s): P76522, P76949
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: January 20, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

About two-thirds of the lipid A residues of cells grown at 12 degrees Celsius are acylated with palmitoleate rather than laurate.1 Publication

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.