ID LPXB_FRAP2 Reviewed; 380 AA. AC B0TXG8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Lipid-A-disaccharide synthase {ECO:0000255|HAMAP-Rule:MF_00392}; DE EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392}; GN Name=lpxB {ECO:0000255|HAMAP-Rule:MF_00392}; GN OrderedLocusNames=Fphi_1201; OS Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / FSC 153 / OS O#319-036). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=484022; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25017 / FSC 153 / O#319-036; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Richardson P.; RT "Complete sequence of chromosome of Francisella philomiragia subsp. RT philomiragia ATCC 25017."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3- CC diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor CC of lipid A, a phosphorylated glycolipid that anchors the CC lipopolysaccharide to the outer membrane of the cell. CC {ECO:0000255|HAMAP-Rule:MF_00392}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D- CC glucosamine = a lipid A disaccharide + H(+) + UDP; CC Xref=Rhea:RHEA:67828, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:137748, ChEBI:CHEBI:176338, ChEBI:CHEBI:176343; CC EC=2.4.1.182; Evidence={ECO:0000255|HAMAP-Rule:MF_00392}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00392}. CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP- CC Rule:MF_00392}. 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; CP000937; ABZ87426.1; -; Genomic_DNA. DR AlphaFoldDB; B0TXG8; -. DR SMR; B0TXG8; -. DR CAZy; GT19; Glycosyltransferase Family 19. DR KEGG; fph:Fphi_1201; -. DR eggNOG; COG0763; Bacteria. DR HOGENOM; CLU_036577_3_0_6; -. DR UniPathway; UPA00973; -. DR GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01635; Glycosyltransferase_GTB-type; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR HAMAP; MF_00392; LpxB; 1. DR InterPro; IPR003835; Glyco_trans_19. DR NCBIfam; TIGR00215; lpxB; 1. DR PANTHER; PTHR30372; LIPID-A-DISACCHARIDE SYNTHASE; 1. DR PANTHER; PTHR30372:SF7; LIPID-A-DISACCHARIDE SYNTHASE; 1. DR Pfam; PF02684; LpxB; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. PE 3: Inferred from homology; KW Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis; KW Lipid metabolism; Transferase. FT CHAIN 1..380 FT /note="Lipid-A-disaccharide synthase" FT /id="PRO_1000080279" SQ SEQUENCE 380 AA; 43415 MW; 9A695C990BAAB4CA CRC64; MRIGIVAGEL SGDQLGATLV EALKKKYPNA EIEGIGGPKM EAQGFKSLYP MDALSLIGFL EILSKGLSIL NIRRKIIKYF KHNKPDIFIG IDAPDFNLTV EKKLRASGIK TIHYVSPKIW VWREYRIKKI RKATDKILAI LPFEVEYYKN RHNFEAIYVG HPLAKNISLE IDRSKYKKRL GLENVELPIL SVLPGSRTTE VTRLLPLFLD AIEKLQESGY KFKAIMPLAK PSLKPIFDQY NSQIRSLGIE VLETNSHDVL KASDLSLLAS GTATLEAMLC KLPMVVGYKL SKLSAFIGRI LIRGHSYWAF PNILHKSEII KELIQEDCTV DNLFYELKRL FDDKQRNNYI VQEFKKIHEH MVVDTEEKII EVLDSIIEKS //