ID   LPXB1_LEGPA             Reviewed;         384 AA.
AC   Q5X5J5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=lpp1325;
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}.
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DR   EMBL; CR628336; CAH12476.1; -; Genomic_DNA.
DR   RefSeq; WP_011213667.1; NC_006368.1.
DR   AlphaFoldDB; Q5X5J5; -.
DR   SMR; Q5X5J5; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; lpp:lpp1325; -.
DR   LegioList; lpp1325; -.
DR   HOGENOM; CLU_036577_3_1_6; -.
DR   OMA; PTVWAWR; -.
DR   BRENDA; 2.4.1.182; 2943.
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..384
FT                   /note="Lipid-A-disaccharide synthase 1"
FT                   /id="PRO_0000255192"
SQ   SEQUENCE   384 AA;  42761 MW;  00BDB82CDA3FC24C CRC64;
     MPNASRVVIV AGEESGDHHA AELVKQLKAV YPNLKISGIG GKHLRAAGVH LISDLTRYAV
     TGLTEIIPFL KIFHKAFQDI KQHLSTQKPD LLILVDYPAF NLRLAKYAKK KLGLKIIYYI
     SPQIWAWKGK RIHLIKDSID KMAVIFPFEK TIYENAGVPV SFVGHPLVKK IASAKDKHSS
     RTFLGLPLDE PIIALLPGSR HSEIERHIPI LVNTAKLLTL DNPKLRFVVP IAGTINPDKV
     KAYFSNQNLT VTFIQGQAIE CMSAADFVIV ASGTASLECA LLEKPMCIIY KSSFLTYVAA
     MYFIKVKFLG LCNLLANKMM VPEFLQYDCN EIELSRYISN FHSDPNQPKS MINQLAKLKE
     SLSSSQADCS LFDLVVAELP EKNA