ID LPXA_BURTA Reviewed; 262 AA. AC Q2SWY6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 105. 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=BTH_I2039; OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / OS CIP 106301 / E264). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264; RX PubMed=16336651; DOI=10.1186/1471-2164-6-174; RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., RA DeShazer D.; RT "Bacterial genome adaptation to niches: divergence of the potential RT virulence genes in three Burkholderia species of different survival RT strategies."; RL BMC Genomics 6:174-174(2005). 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; CP000086; ABC38675.1; -; Genomic_DNA. DR RefSeq; WP_009890458.1; NZ_CP008785.1. DR PDB; 4EQY; X-ray; 1.80 A; A/B/C/E/F/G=1-262. DR PDBsum; 4EQY; -. DR AlphaFoldDB; Q2SWY6; -. DR SMR; Q2SWY6; -. DR GeneID; 66547473; -. DR KEGG; bte:BTH_I2039; -. DR HOGENOM; CLU_061249_0_0_4; -. DR UniPathway; UPA00359; UER00477. DR Proteomes; UP000001930; Chromosome I. 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; 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 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Cytoplasm; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Repeat; Transferase. FT CHAIN 1..262 FT /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine FT O-acyltransferase" FT /id="PRO_1000013160" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:4EQY" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:4EQY" FT STRAND 63..66 FT /evidence="ECO:0007829|PDB:4EQY" FT STRAND 79..82 FT /evidence="ECO:0007829|PDB:4EQY" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:4EQY" FT TURN 99..102 FT /evidence="ECO:0007829|PDB:4EQY" FT STRAND 103..107 FT /evidence="ECO:0007829|PDB:4EQY" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:4EQY" FT STRAND 181..184 FT /evidence="ECO:0007829|PDB:4EQY" FT TURN 185..188 FT /evidence="ECO:0007829|PDB:4EQY" FT STRAND 189..193 FT /evidence="ECO:0007829|PDB:4EQY" FT HELIX 195..200 FT /evidence="ECO:0007829|PDB:4EQY" FT HELIX 205..219 FT /evidence="ECO:0007829|PDB:4EQY" FT HELIX 225..235 FT /evidence="ECO:0007829|PDB:4EQY" FT STRAND 238..240 FT /evidence="ECO:0007829|PDB:4EQY" FT HELIX 243..254 FT /evidence="ECO:0007829|PDB:4EQY" SQ SEQUENCE 262 AA; 27874 MW; 189A5441A77BB522 CRC64; MSRIHPTAII EPGAQLHETV EVGPYAIVGS NVTIGARTTI GSHSVIEGHT TIGEDNRIGH YASVGGRPQD MKYKDEPTRL VIGDRNTIRE FTTIHTGTVQ DAGVTTLGDD NWIMAYVHIG HDCRVGSHVV LSSNAQMAGH VEIGDWAIVG GMSGVHQYVR IGAHSMLGGA SALVQDIPPF VIAAGNKAEP HGINVEGLRR RGFSPDAISA LRSAYRILYK NSLSLEEAKV QLSELAQAGG DGDAAVKALV DFVESSQRGI IR //