ID LPXB_PROMI Reviewed; 141 AA. AC P72216; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 62. DE RecName: Full=Lipid-A-disaccharide synthase; DE EC=2.4.1.182; DE Flags: Fragment; GN Name=lpxB; OS Proteus mirabilis. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Proteus. OX NCBI_TaxID=584; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=PR 990; RA Servos S., Khan S.A., Papakonstantinopoulou A., Dougan G., Maskell D.; RL Submitted (NOV-1996) 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. {ECO:0000250}. 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 -!- 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; 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. CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000305}. 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; Y09263; CAA70457.1; -; Genomic_DNA. DR AlphaFoldDB; P72216; -. DR SMR; P72216; -. DR STRING; 584.AOUC001_03425; -. DR CAZy; GT19; Glycosyltransferase Family 19. DR UniPathway; UPA00359; UER00481. DR GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-EC. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW. 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..>141 FT /note="Lipid-A-disaccharide synthase" FT /id="PRO_0000190175" FT NON_TER 141 SQ SEQUENCE 141 AA; 15814 MW; 551D19F25600561E CRC64; MTLSGQSSIK QRPLVIGLVA GETSGDILGA GLIRALKQMH PNIRFVGVAG PLMQAEGCEA WYEMEELAVM GIVEVLERLP RLLKIRKDLT QRFTQLKPDV FVGIDAPDFN ITLEGRLKQK GLKTIHYVSP SVWAWRQKRV F //