ID   LPXB2_LEGPL             Reviewed;         385 AA.
AC   Q5WSK6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 93.
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};
GN   OrderedLocusNames=lpl2872;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
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}.
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DR   EMBL; CR628337; CAH17116.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5WSK6; -.
DR   SMR; Q5WSK6; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; lpf:lpl2872; -.
DR   LegioList; lpl2872; -.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   BRENDA; 2.4.1.182; 2943.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002517; 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   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..385
FT                   /note="Lipid-A-disaccharide synthase 2"
FT                   /id="PRO_0000255191"
SQ   SEQUENCE   385 AA;  43707 MW;  1D98923F1C9B3E5B CRC64;
     MIKKRQTRIA MIAGEMSGDL LGAGVIRELK KHLKNVEFIG VGGPQMLEEG FQSLANMSEL
     SVMGISDVLR RYPQLYFIRE RLLKEWTINP PDVFIGIDYP DFNLSVETRL KRQNVKTVHL
     VSPKVWAWRQ KRVYLIKKAV DLVLTLFPFE ESFYQQYDVP AQFVGHPLAD LIEINPNNAD
     LRKKYNYKPD DTILAVLPGS RIGEIKYIGP LFLEVMQRIA VEMPHVHFIV PIACQELYPV
     FFKQFQARYS HLKIQIIQGN AREAMAISDV VLTKSGTATL EAMLLKRPMV VAFKWSKFTH
     AIIAPQVKIP YVALPNLLAN KKLVPEFVQE KATANSITES VLNLLACPSQ SNLNKQFTAI
     HHTLRQNANE KAALSILKIL ETSSA
//