ID LPXA_YEREN Reviewed; 262 AA. AC P32201; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 13-SEP-2023, entry version 104. 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}; OS Yersinia enterocolitica. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=630; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=EH902; RX PubMed=8293817; DOI=10.1016/0014-5793(94)80211-4; RA Vuorio R., Haerkonen T., Tolvanen M., Vaara M.; RT "The novel hexapeptide motif found in the acyltransferases LpxA and LpxD of RT lipid A biosynthesis is conserved in various bacteria."; RL FEBS Lett. 337:289-292(1994). 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. 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. 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; Z25463; CAA80953.1; -; Genomic_DNA. DR PIR; S41753; S41753. DR AlphaFoldDB; P32201; -. DR SMR; P32201; -. DR STRING; 1443113.LC20_01207; -. DR eggNOG; COG1043; Bacteria. DR UniPathway; UPA00359; UER00477. 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; 2. PE 3: Inferred from homology; KW Acyltransferase; Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis; KW Lipid metabolism; Repeat; Transferase. FT CHAIN 1..262 FT /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine FT O-acyltransferase" FT /id="PRO_0000188080" SQ SEQUENCE 262 AA; 27986 MW; 0DA803DE1E08A59C CRC64; MIDKTAVIHP SSIVEEGAVI GAGVHIGPFC FVGSQVEIGA GTELKSHVVV NGITKIGCDN QIYQFASIGE ANQDLKYAGE PTRVEIGDRN RIRESVSIHR GTVQGGGLSK VGSDNLLMIN AHIAHDCIIG DRCILANNAT LGGHVEIDDF AIIGGMTAIH QFCVIGAHVM VGGCSGVAQD VPPFVIAQGN HATPFGINIE GLKRRGFDKE SLHAIRNAYK LLYRSGRTLD EVKPEIAELA DQHPAVQAFI DFFARSTRGI IR //