Reviewed, UniProtKB/Swiss-Prot P32199 (LPXA_RICRI)

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

Organism

Rickettsia rickettsii

Taxonomic identifier

783 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group

Protein attributes

Sequence length	264 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 MF_00387
Catalytic activity	(R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetylglucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine. HAMAP 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 MF_00387
Subunit structure	Homotrimer By similarity.
Subcellular location	Cytoplasm. HAMAP MF_00387
Sequence similarities	Belongs to the transferase hexapeptide repeat family. LpxA subfamily.

Ontologies

Keywords
Biological process	Lipid A biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Domain	Repeat
Molecular function	Acyltransferase Transferase
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 – 264	264	Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP MF_00387		PRO_0000188066

Sequences

	Sequence		Length	Mass (Da)
	P32199-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 7A24B38C76A596D0	FASTA	264	28,333
	10 20 30 40 50 60 MSNSNIHTTA VIAEGAKLGK NVKIGPYCII GPEVVLNDNV ELKSHVVIEG ITEIGENTVI 70 80 90 100 110 120 YPFASIGQPP QILKYANERS STIIGSNNTI REYVTVQAGS QGGGMMTRVG NNNLFMVGVH 130 140 150 160 170 180 IGHDCKIGNN VVFANYVSLA GHIGVGDYAI IGGLSAVHQY ARIGEYSMIG GLSPVGADVI 190 200 210 220 230 240 PFGLVSSKRA VLEGLNLIGM NRKGFDKVKS LSALKAIEEI FSGEGNFAER IKQVAEKYNN 250 260 NSIVIQIIDF LNQDSSRAFC RFEK

References

[1]	"Characterization of a Rickettsia rickettsii DNA fragment analogous to the fir A-ORF17-lpxA region of Escherichia coli." Shaw E.I., Wood D.O. Gene 140:109-113(1994) [PubMed: 8125326] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	L22690 Genomic DNA. Translation: AAA26386.1.
3D structure databases
HSSP	HSSP built from PDB template 1LXA based on UniProtKB P10440.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.129. 292822.
Family and domain databases
HAMAP	MF_00387. [Tree]
InterPro	IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR010137. Lipid_A_lpxA. [Graphical view]
Pfam	PF00132. Hexapep. 7 hits. [Graphical view]
PIRSF	PIRSF000456. UDP-GlcNAc_acltr. 1 hit.
TIGRFAMs	TIGR01852. lipid_A_lpxA. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LPXA_RICRI

Accession

Primary (citable) accession number: P32199

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	September 22, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)