ID   LPXB2_LEGPA             Reviewed;         385 AA.
AC   Q5X0T2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Lipid-A-disaccharide synthase 2 {ECO:0000255|HAMAP-Rule:MF_00392};
DE            EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392};
GN   Name=lpxB2 {ECO:0000255|HAMAP-Rule:MF_00392}; OrderedLocusNames=lpp3014;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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}.
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; CR628336; CAH14167.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5X0T2; -.
DR   SMR; Q5X0T2; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; lpp:lpp3014; -.
DR   LegioList; lpp3014; -.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; EWTINPP; -.
DR   UniPathway; UPA00973; -.
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..385
FT                   /note="Lipid-A-disaccharide synthase 2"
FT                   /id="PRO_0000255193"
SQ   SEQUENCE   385 AA;  43681 MW;  53F65F52047322C3 CRC64;
     MIKEKRLRIA MVAGELSGDL LGAGVIRELK QHLTNVEFMG VGGPQMLKEG FHSLIDISEL
     SVMGISDVLR RYPQLYLIRE RLLREWTINP PDVFIGIDYP DFNLSVEARL KKQHIKTIHL
     VSPKVWAWRQ KRVHLIKKAV DLVLTLFPFE EAFYLQHGVS AQFIGHPLAD LIEINPSCSA
     LRKKYNYHSD DTILAVLPGS RVGEIKYMGP LFLEVMQRIA MERPHVHFIV PIACQDLYPV
     FFKQLHAEYD YLKIQVIQGN AREAMAISDV VLTKSGTATL EAMLLKRPMV VAFKWGILTH
     AIIAPQVKVP YIALPNLLAG KKLIPEFVQE KANVDSITES VLNLLDSSNQ NELIKQFTDI
     HRTLRQNANE KAALAILRIL EDSLT