ID LPXB_ECO7I Reviewed; 382 AA. AC B7NIE4; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 71. 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=ECIAI39_0185; OS Escherichia coli O7:K1 (strain IAI39 / ExPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IAI39 / ExPEC; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E., RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). 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=2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl CC 1-phosphate + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D- CC glucosamine = H(+) + lipid A disaccharide (E. coli) + UDP; CC Xref=Rhea:RHEA:22668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57957, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58466, ChEBI:CHEBI:78847; CC Evidence={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: 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 5/6. {ECO:0000255|HAMAP- CC 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; CU928164; CAR16325.1; -; Genomic_DNA. DR RefSeq; WP_000139673.1; NC_011750.1. DR RefSeq; YP_002406231.1; NC_011750.1. DR AlphaFoldDB; B7NIE4; -. DR SMR; B7NIE4; -. DR STRING; 585057.ECIAI39_0185; -. DR CAZy; GT19; Glycosyltransferase Family 19. DR KEGG; ect:ECIAI39_0185; -. DR PATRIC; fig|585057.6.peg.198; -. DR HOGENOM; CLU_036577_3_0_6; -. DR UniPathway; UPA00359; UER00481. DR Proteomes; UP000000749; Chromosome. 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 HAMAP; MF_00392; LpxB; 1. DR InterPro; IPR003835; Glyco_trans_19. 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..382 FT /note="Lipid-A-disaccharide synthase" FT /id="PRO_1000191482" SQ SEQUENCE 382 AA; 42385 MW; CB6EB5066438AD9D CRC64; MTEQRPLTIA LVAGETSGDI LGAGLIRALK ERVPNARFVG VAGPRMQAEG CEAWYEMEEL AVMGIVEVLG RLRRLLHIRA DLTKRFGELK PDVFVGIDAP DFNITLEGNL KKQGIKTIHY VSPSVWAWRQ KRVFKIGRAT DLVLAFLPFE KAFYDKYNVP CRFIGHTMAD AMPLDPDKNG ARDVLGIPHD AHCLALLPGS RGAEVEMLSA DFLKTAQLLR QTYPDLEIVV PLVNAKRREQ FERIKAEVAP DLAVHLLDGM GREAMVASDA ALLASGTAAL ECMLAKCPMV VGYRMKPFTF WLAKRLVKTE YVSLPNLLAG RELVKELLQE ECEPQKLAAA LLPLLANGKT SHAMHDTFRE LHQQIRCNAD EQAAQAVLEL AQ //