ID   LPXB_FRATT              Reviewed;         380 AA.
AC   Q5NEQ2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=FTT_1568c;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
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}.
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DR   EMBL; AJ749949; CAG46201.1; -; Genomic_DNA.
DR   RefSeq; WP_003014884.1; NZ_CP010290.1.
DR   RefSeq; YP_170490.1; NC_006570.2.
DR   AlphaFoldDB; Q5NEQ2; -.
DR   SMR; Q5NEQ2; -.
DR   STRING; 177416.FTT_1568c; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   DNASU; 3191793; -.
DR   EnsemblBacteria; CAG46201; CAG46201; FTT_1568c.
DR   KEGG; ftu:FTT_1568c; -.
DR   eggNOG; COG0763; Bacteria.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001174; 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; Reference proteome; Transferase.
FT   CHAIN           1..380
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255182"
SQ   SEQUENCE   380 AA;  43088 MW;  82D4B01962B0DF9C CRC64;
     MRIGIVAGEL SGDQLGGTLV EALKQKYPNA IIEGIGGPKM AAAGFKSLYP MDALSLIGFL
     EIISKGLRIL SIRRKIINYF KQNKPDIFIG IDAPDFNLTV EKELRSAGIK TIHYVSPKIW
     VWREYRIKKI RKATDKILAI LPFETEYYKN RHKFEAIYVG HPLAKNIPIH IDRAKYRDKL
     GLKGSSLPIL SVLPGSRTTE VSRLLPLFLL ALQKLVDAGY KFKAIMPLAK PSLKPLFAKY
     KEQIDSLGIE VFETNSHDVL KASDLSLLAS GTATLEAMLC KLPMVVGYKL SWLSALIGRM
     LIGNHSYWAF PNILHKNEII KELIQEDCTV DNLFSELKRL FDDKRRNDYI VEEFEKIHKE
     MVIDTESKII QVLDTMIEKS