P32200 (LPXA_SALTY) 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:	STM0228

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

Protein attributes

Sequence length	262 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. 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 HAMAP-Rule MF_00387.
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	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 – 262	262	Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387		PRO_0000188068

Sequences

	Sequence		Length	Mass (Da)
	P32200 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: C5C8E15ED7C6F270	FASTA	262	28,089
	10 20 30 40 50 60 MIDKSAFIHP TAIVEDGAVI GANAHIGPFC IVGPQVEIGE GTVLKSHVVV NGQTKIGRDN 70 80 90 100 110 120 EIYQFASIGE VNQDLKYAGE PTRVEIGDRN RIRESVTIHR GTVQGGGLTK VGSDNLLMIN 130 140 150 160 170 180 AHVAHDCTVG NRCILANNAT LAGHVSVDDF AIIGGMTAVH QFCIIGAHVM VGGCSGVAQD 190 200 210 220 230 240 VPPYVIAQGN HATPFGVNIE GLKRRGFSRE GLVAIRNAYK LLYRSGKTLD EAKLEIAELA 250 260 EKHPEVKAFT EFFERSTRGP IR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The novel hexapeptide motif found in the acyltransferases LpxA and LpxD of lipid A biosynthesis is conserved in various bacteria." Vuorio R., Haerkonen T., Tolvanen M., Vaara M. FEBS Lett. 337:289-292(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT2 / SH5014.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z25462 Genomic DNA. Translation: CAA80950.1. AE006468 Genomic DNA. Translation: AAL19192.1.
PIR	S41751.
RefSeq	NP_459233.1. NC_003197.1.
3D structure databases
ProteinModelPortal	P32200.
SMR	P32200. Positions 1-262.
ModBase	Search...
Protein-protein interaction databases
STRING	99287.STM0228.
Proteomic databases
PRIDE	P32200.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL19192; AAL19192; STM0228.
GeneID	1251746.
KEGG	stm:STM0228.
PATRIC	32378743. VBISalEnt20916_0241.
Phylogenomic databases
HOGENOM	HOG000294326.
KO	K00677.
OMA	REFCTFN.
ProtClustDB	PRK05289.
Enzyme and pathway databases
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. 5 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. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LPXA_SALTY

Accession

Primary (citable) accession number: P32200

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program