Q9PIM1 (LPXA_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
Short name=UDP-N-acetylglucosamine acyltransferase
EC=2.3.1.129

Gene names

Name:	lpxA
Ordered Locus Names:	Cj0274

Organism

Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]

Taxonomic identifier

192222 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter › Campylobacter jejuni › Campylobacter jejuni subsp. jejuni

Protein attributes

Sequence length	263 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell By similarity. HAMAP-Rule MF_00387
Catalytic activity	(R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D-glucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine. HAMAP-Rule MF_00387
Pathway	Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6. HAMAP-Rule MF_00387
Subunit structure	Homotrimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the transferase hexapeptide repeat family. LpxA subfamily.

Ontologies

Keywords
Biological process	Lipid A biosynthesis Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Domain	Repeat
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid A biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 263

263

Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387

PRO_0000188038

Secondary structure

1

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263

Helix Strand Turn

Details...

Beta strand

63 – 66

4

Beta strand

80 – 83

4

Beta strand

94 – 96

3

Turn

100 – 103

4

Beta strand

104 – 108

5

Beta strand

182 – 185

4

Beta strand

190 – 194

5

Helix

196 – 202

7

Helix

205 – 219

15

Beta strand

220 – 222

3

Helix

224 – 232

9

Helix

238 – 249

12

Sequences

	Sequence		Length	Mass (Da)
	Q9PIM1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: C3D17D1BE12F9F01	FASTA	263	28,651
	10 20 30 40 50 60 MKKIHPSAVI EEGAQLGDDV VIEAYAYVSK DAKIGNNVVI KQGARILSDT TIGDHSRVFS 70 80 90 100 110 120 YAIVGDIPQD ISYKEEQKSG VVIGKNATIR EFATINSGTA KGDGFTRIGD NAFIMAYCHI 130 140 150 160 170 180 AHDCLLGNNI ILANNATLAG HVELGDFTVV GGLTPIHQFV KVGEGCMIAG ASALSQDIVP 190 200 210 220 230 240 FCLAEGNRAS IRSLNLVGIR RRFDKDEVDR LSRAFKTLFR QGDLKENAKN LLENQESENV 250 260 KKMCHFILET KRGIPVYRGK NNA

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL111168 Genomic DNA. Translation: CAL34428.1.

PIR

A81446.

RefSeq

YP_002343716.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3R0S	X-ray	2.30	A	1-263	[»]

ProteinModelPortal

Q9PIM1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9PIM1. 29 interactions.

STRING

192222.Cj0274.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAL34428; CAL34428; Cj0274.

GeneID

904599.

KEGG

cje:Cj0274.

PATRIC

20057469. VBICamJej33762_0268.

Phylogenomic databases

eggNOG

COG1043.

HOGENOM

HOG000294326.

KO

K00677.

OMA

REFCTFN.

ProtClustDB

PRK05289.

Enzyme and pathway databases

BioCyc

CJEJ192222:GJTS-254-MONOMER.

UniPathway

UPA00359; UER00477.

Family and domain databases

HAMAP

MF_00387. LpxA.

InterPro

IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR010137. Lipid_A_LpxA.
IPR011004. Trimer_LpxA-like.
[Graphical view]

Pfam

PF00132. Hexapep. 3 hits.
[Graphical view]

PIRSF

PIRSF000456. UDP-GlcNAc_acltr. 1 hit.

SUPFAM

SSF51161. Trimer_LpxA_like. 1 hit.

TIGRFAMs

TIGR01852. lipid_A_lpxA. 1 hit.

PROSITE

PS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

LPXA_CAMJE

Accession

Primary (citable) accession number: Q9PIM1
Secondary accession number(s): Q0PBN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program