ID   LPXB_FRATN              Reviewed;         380 AA.
AC   A0Q7X9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=FTN_1477;
OS   Francisella tularensis subsp. novicida (strain U112).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=401614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U112;
RX   PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA   Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA   Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA   Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA   Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA   Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA   Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT   "Comparison of Francisella tularensis genomes reveals evolutionary events
RT   associated with the emergence of human pathogenic strains.";
RL   Genome Biol. 8:R102.1-R102.16(2007).
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; CP000439; ABK90344.1; -; Genomic_DNA.
DR   RefSeq; WP_003040462.1; NZ_CP009633.1.
DR   AlphaFoldDB; A0Q7X9; -.
DR   SMR; A0Q7X9; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ABK90344; ABK90344; FTN_1477.
DR   KEGG; ftn:FTN_1477; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   BioCyc; FTUL401614:G1G75-1525-MON; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000762; 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..380
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000049397"
SQ   SEQUENCE   380 AA;  43117 MW;  D1CF476843C10ED4 CRC64;
     MRIGIVAGEL SGDQLGGTLV EALKQKYPNA IIEGIGGPKM AAAGFKSLYP MDALSLIGFL
     EIISKGLRIL SIRRKIINYF KQNKPDIFIG IDAPDFNLTV EKELRSVGIK TIHYVSPKIW
     VWREYRIKKI RKATDKILAI LPFETEYYKN RHKFEAIYVG HPLAKNIPIH IDRTKYRDKL
     GLKGNSLPIL SVLPGSRTTE VSRLLPLFLL ALQKLVDAGY KFKAIMPLAK PSLKPLFAKY
     KEQIDSLGIE VFETNSHDVL KASDLSLLAS GTATLEAMLC KLPMVVGYKL SWLSALIGRM
     LIGNHSYWAF PNILHKSEII KELIQEDCTV DNLFSELKRL FDDKQRNDYI VEEFEKIHKE
     MVIDTESKII QVLNTMIEKS