ID   LPXB_ECOHS              Reviewed;         382 AA.
AC   A7ZWC8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
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}; OrderedLocusNames=EcHS_A0184;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000802; ABV04582.1; -; Genomic_DNA.
DR   RefSeq; WP_000139654.1; NC_009800.1.
DR   AlphaFoldDB; A7ZWC8; -.
DR   SMR; A7ZWC8; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; ecx:EcHS_A0184; -.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00359; UER00481.
DR   Proteomes; UP000001123; 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   HAMAP; MF_00392; LpxB; 1.
DR   InterPro; IPR003835; Glyco_trans_19.
DR   PANTHER; PTHR30372; PTHR30372; 1.
DR   Pfam; PF02684; LpxB; 1.
DR   TIGRFAMs; TIGR00215; lpxB; 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_1000060770"
SQ   SEQUENCE   382 AA;  42382 MW;  12C76B6ECA438B47 CRC64;
     MTEQRPLTIA LVAGETSGDI LGAGLIRALK EHVPNARFVG VAGPRMQAEG CEAWYEMEEL
     AVMGIVEVLG RLRRLLHIRA DLTKRFGELK PDVFVGIDAP DFNITLEGNL KKQGIKTIHY
     VSPSVWAWRQ KRVFKIGRAT DLVLAFLPFE KAFYDKYNVP CRFIGHTMAD AMPLDPDKNA
     ARDVLGIPHD AHCLALLPGS RGAEVEMLSA DFLKTAQLLR QTYPDLEIVV PLVNAKRREQ
     FERIKAEVAP DLSVHLLDGM GREAMVASDA ALLASGTAAL ECMLAKCPMV VGYRMKPFTF
     WLAKRLVKTD YVSLPNLLAG RELVKELLQE ECEPQKLAAA LLPLLANGKT SHAMHDTFRE
     LHQQIRCNAD EQAAQAVLEL AQ