ID LPXA_BRUA1 Reviewed; 278 AA. AC B2S601; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387}; DE Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387}; DE EC=2.3.1.129 {ECO:0000255|HAMAP-Rule:MF_00387}; GN Name=lpxA {ECO:0000255|HAMAP-Rule:MF_00387}; GN OrderedLocusNames=BAbS19_I10910; OS Brucella abortus (strain S19). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=430066; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S19; RX PubMed=18478107; DOI=10.1371/journal.pone.0002193; RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S., RA Bricker B., Yu G., Du L., Sobral B.W.; RT "Genome sequence of Brucella abortus vaccine strain S19 compared to RT virulent strains yields candidate virulence genes."; RL PLoS ONE 3:E2193-E2193(2008). CC -!- FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated CC glycolipid that anchors the lipopolysaccharide to the outer membrane of CC the cell. {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = CC a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo- CC [ACP]; Xref=Rhea:RHEA:67812, Rhea:RHEA-COMP:9685, Rhea:RHEA- CC COMP:9945, ChEBI:CHEBI:57705, ChEBI:CHEBI:64479, ChEBI:CHEBI:78827, CC ChEBI:CHEBI:173225; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00387}; CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N- CC acetyl-alpha-D-glucosamine: step 1/6. {ECO:0000255|HAMAP- CC Rule:MF_00387}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00387}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000887; ACD72598.1; -; Genomic_DNA. DR RefSeq; WP_002964279.1; NC_010742.1. DR AlphaFoldDB; B2S601; -. DR SMR; B2S601; -. DR GeneID; 58775764; -. DR KEGG; bmc:BAbS19_I10910; -. DR HOGENOM; CLU_061249_0_0_5; -. DR UniPathway; UPA00359; UER00477. DR Proteomes; UP000002565; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd03351; LbH_UDP-GlcNAc_AT; 1. DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1. DR Gene3D; 1.20.1180.10; Udp N-acetylglucosamine O-acyltransferase, C-terminal domain; 1. DR HAMAP; MF_00387; LpxA; 1. DR InterPro; IPR029098; Acetyltransf_C. DR InterPro; IPR037157; Acetyltransf_C_sf. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR010137; Lipid_A_LpxA. DR InterPro; IPR011004; Trimer_LpxA-like_sf. DR NCBIfam; TIGR01852; lipid_A_lpxA; 1. DR PANTHER; PTHR43480; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE; 1. DR PANTHER; PTHR43480:SF1; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF13720; Acetyltransf_11; 1. DR Pfam; PF00132; Hexapep; 2. DR PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1. DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase; Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis; KW Lipid metabolism; Repeat; Transferase. FT CHAIN 1..278 FT /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine FT O-acyltransferase" FT /id="PRO_1000122686" SQ SEQUENCE 278 AA; 29386 MW; DF77C706EEA9F8DF CRC64; MKETFIHPTA LVEPGVELGQ GVSVGPFCHV QSGAIIGNDC ELMSHVVITG ATTLGAGTKV YPHAILGCDP QNNKHKGGPT RLNVGVNCII REGVTMHKGS DNARGYTSIG DNCSFLAYAH VAHDCDIGDY VTFSNNVMIG GHTSIGHHAI LGGGAAVHQF VRVGHHAFIG GLAAVVSDLI PYGMAIGVHA HLGGLNIIGM KRSGMERKEI HNLRHAVRML FDRTKPIRQR AQDVLAAIPD SPTVSDMISF INVDTKRAYC TPPLDAAHGG AGHDSDED //