ID   LPXB2_LEGPH             Reviewed;         385 AA.
AC   Q5ZRD7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=lpg2945;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(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; AE017354; AAU28991.1; -; Genomic_DNA.
DR   RefSeq; YP_096938.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZRD7; -.
DR   SMR; Q5ZRD7; -.
DR   STRING; 272624.lpg2945; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PaxDb; Q5ZRD7; -.
DR   EnsemblBacteria; AAU28991; AAU28991; lpg2945.
DR   KEGG; lpn:lpg2945; -.
DR   PATRIC; fig|272624.6.peg.3145; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; EWTINPP; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000609; 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..385
FT                   /note="Lipid-A-disaccharide synthase 2"
FT                   /id="PRO_0000255195"
SQ   SEQUENCE   385 AA;  43476 MW;  0101A96F4DA538F7 CRC64;
     MTMKRPTRIA MVAGELSGDL LGAGVIRELK QHLTNVEFMG VGGPQMLKEG FHSLIDISEL
     SVMGISDVLR RYPQLYLIRE RLLREWTINP PDVFIGIDYP DFNLSVEARL KKQHIKTIHL
     VSPKVWAWRQ KRVHLIKKAV DLVLTLFPFE EAFYRQHGVS AQFIGHPLAD LIEINPSCST
     LRKKYNYHSD DTILAVLPGS RVGEIKYMGP LFLEVMQRIA VERPHVHFIV PIACQDLYPV
     FFKQLHAEYG HLKIQIIQGN AREAMAISDV VLTKSGTATL EAMLLKRPMV VAFKWGILTH
     AIIAPQVKVP YIALPNLLAG KKLIPEFVQE KANVDSITES VLNLLDSSNQ NELIKQFTDI
     HCTLRQNANE KAALSILRIL GTSLT