Q2SWY6 (LPXA_BURTA) 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:	BTH_I2039

Organism

Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]

Taxonomic identifier

271848 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group › Burkholderia thailandensis

Protein attributes

Sequence length	262 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
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 – 262

262

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

PRO_1000013160

Secondary structure

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262

Helix Strand Turn

Details...

Beta strand

32 – 34

3

Beta strand

48 – 52

5

Beta strand

63 – 66

4

Beta strand

79 – 82

4

Beta strand

93 – 95

3

Turn

99 – 102

4

Beta strand

103 – 107

5

Beta strand

175 – 177

3

Beta strand

181 – 184

4

Turn

185 – 188

4

Beta strand

189 – 193

5

Helix

195 – 200

6

Helix

205 – 219

15

Helix

225 – 235

11

Beta strand

238 – 240

3

Helix

243 – 254

12

Sequences

	Sequence		Length	Mass (Da)
	Q2SWY6 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 189A5441A77BB522	FASTA	262	27,874
	10 20 30 40 50 60 MSRIHPTAII EPGAQLHETV EVGPYAIVGS NVTIGARTTI GSHSVIEGHT TIGEDNRIGH 70 80 90 100 110 120 YASVGGRPQD MKYKDEPTRL VIGDRNTIRE FTTIHTGTVQ DAGVTTLGDD NWIMAYVHIG 130 140 150 160 170 180 HDCRVGSHVV LSSNAQMAGH VEIGDWAIVG GMSGVHQYVR IGAHSMLGGA SALVQDIPPF 190 200 210 220 230 240 VIAAGNKAEP HGINVEGLRR RGFSPDAISA LRSAYRILYK NSLSLEEAKV QLSELAQAGG 250 260 DGDAAVKALV DFVESSQRGI IR

References

[1]

"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies." Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D. BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000086 Genomic DNA. Translation: ABC38675.1.

RefSeq

YP_442563.1. NC_007651.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4EQY	X-ray	1.80	A/B/C/E/F/G	1-262	[»]

ProteinModelPortal

Q2SWY6.

SMR

Q2SWY6. Positions 2-262.

ModBase

Search...

Protein-protein interaction databases

STRING

271848.BTH_I2039.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

ABC38675; ABC38675; BTH_I2039.

GeneID

3848943.

KEGG

bte:BTH_I2039.

PATRIC

19307120. VBIBurTha36512_4849.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG1043.

HOGENOM

HOG000294326.

KO

K00677.

OMA

REFCTFN.

ProtClustDB

PRK05289.

Enzyme and pathway databases

BioCyc

BTHA271848:GJMY-2040-MONOMER.

UniPathway

UPA00359; UER00477.

Family and domain databases

HAMAP

MF_00387. LpxA.

InterPro

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

Pfam

PF00132. Hexapep. 4 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_BURTA

Accession

Primary (citable) accession number: Q2SWY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program