ID   LPXB1_LEGPL             Reviewed;         384 AA.
AC   Q5WWX7;
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 1 {ECO:0000255|HAMAP-Rule:MF_00392};
DE            EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392};
GN   Name=lpxB1 {ECO:0000255|HAMAP-Rule:MF_00392}; OrderedLocusNames=lpl1322;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; 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; CAH15562.1; -; Genomic_DNA.
DR   RefSeq; WP_011215392.1; NC_006369.1.
DR   AlphaFoldDB; Q5WWX7; -.
DR   SMR; Q5WWX7; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   DNASU; 3114168; -.
DR   EnsemblBacteria; CAH15562; CAH15562; lpl1322.
DR   KEGG; lpf:lpl1322; -.
DR   LegioList; lpl1322; -.
DR   HOGENOM; CLU_036577_3_1_6; -.
DR   OMA; PTVWAWR; -.
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   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..384
FT                   /note="Lipid-A-disaccharide synthase 1"
FT                   /id="PRO_0000255190"
SQ   SEQUENCE   384 AA;  42663 MW;  C6C2C4C471B542B7 CRC64;
     MPNASRVVIV AGEESGDHHA AELVKQLKAV YPDLEISGIG GKHLRAAGVH LISDLTRYAV
     TGLTEIIPFL KIFRKAFQDI KQHLSTQKPD LLILVDYPAF NLRLAKYAKK KLGLKIIYYI
     SPQIWAWKGK RIHLIKDCID KMAVIFPFEK TIYENAGVPV SFVGHPLVKK IAAAKDKHSS
     RTSLGLPLNE PIIALLPGSR HSEIERHIPI LVNTAKLLTL DSPKLRFVVP IAGTINPDKV
     KAYFSNQNLT VTFIQGQAIE CMSAADFVIV ASGTASLECA LLEKPMCIIY KSSFLTYVAA
     MYFIKVKFLG LCNLLANKMM VPEFLQYDCN AIELSRYISN FHNNPNQPES MINQLAKLKE
     SLSSSQADCS LFDLVVAELP EKNA