Q2YRQ5 (LPXA_BRUA2) 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:	BAB1_1173

Organism

Brucella abortus (strain 2308) [Complete proteome] [HAMAP]

Taxonomic identifier

359391 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus

Protein attributes

Sequence length	278 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 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.
Sequence caution	The sequence AAA96791.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipid A biosynthesis Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Domain	Repeat
Molecular function	Acyltransferase Transferase
Technical term	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 – 278	278	Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase HAMAP-Rule MF_00387		PRO_0000188035
Experimental info
	Sequence conflict	129	1	D → GH Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q2YRQ5 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: DF77C706EEA9F8DF	FASTA	278	29,386
	10 20 30 40 50 60 MKETFIHPTA LVEPGVELGQ GVSVGPFCHV QSGAIIGNDC ELMSHVVITG ATTLGAGTKV 70 80 90 100 110 120 YPHAILGCDP QNNKHKGGPT RLNVGVNCII REGVTMHKGS DNARGYTSIG DNCSFLAYAH 130 140 150 160 170 180 VAHDCDIGDY VTFSNNVMIG GHTSIGHHAI LGGGAAVHQF VRVGHHAFIG GLAAVVSDLI 190 200 210 220 230 240 PYGMAIGVHA HLGGLNIIGM KRSGMERKEI HNLRHAVRML FDRTKPIRQR AQDVLAAIPD 250 260 270 SPTVSDMISF INVDTKRAYC TPPLDAAHGG AGHDSDED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequence of the group 1 outer membrane protein of Brucella abortus." Bearden S.W., Ficht T.A. Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Whole-genome analyses of speciation events in pathogenic Brucellae." Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2308.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U51683 Genomic DNA. Translation: AAA96791.1. Different initiation. AM040264 Genomic DNA. Translation: CAJ11129.1.
RefSeq	YP_414564.1. NC_007618.1.
3D structure databases
ProteinModelPortal	Q2YRQ5.
ModBase	Search...
Protein-protein interaction databases
STRING	359391.BAB1_1173.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAJ11129; CAJ11129; BAB1_1173.
GeneID	3788781.
KEGG	bmf:BAB1_1173.
PATRIC	17845303. VBIBruMel86222_1221.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1043.
HOGENOM	HOG000294326.
KO	K00677.
OMA	GDKNLLM.
ProtClustDB	PRK05289.
Enzyme and pathway databases
BioCyc	BMEL359391:GJOQ-1195-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. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LPXA_BRUA2

Accession

Primary (citable) accession number: Q2YRQ5
Secondary accession number(s): P54080, Q57CY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program