ID   LPXB1_LEGPH             Reviewed;         384 AA.
AC   Q5ZVR9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=lpg1371;
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; AAU27453.1; -; Genomic_DNA.
DR   RefSeq; WP_010947101.1; NC_002942.5.
DR   RefSeq; YP_095400.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZVR9; -.
DR   SMR; Q5ZVR9; -.
DR   STRING; 272624.lpg1371; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PaxDb; Q5ZVR9; -.
DR   PRIDE; Q5ZVR9; -.
DR   EnsemblBacteria; AAU27453; AAU27453; lpg1371.
DR   GeneID; 66490503; -.
DR   KEGG; lpn:lpg1371; -.
DR   PATRIC; fig|272624.6.peg.1441; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_1_6; -.
DR   OMA; PTVWAWR; -.
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..384
FT                   /note="Lipid-A-disaccharide synthase 1"
FT                   /id="PRO_0000255194"
SQ   SEQUENCE   384 AA;  42634 MW;  BFC508AFCACD5372 CRC64;
     MPNASRVVIV AGEESGDHHA AELVKQLKAV YPDLEISGIG GKHLRAAGVH LISDLTRYAV
     TGLTEIIPFL KIFRKAFQDI KQHLSTQKPD LLILVDYPAF NLRLAKYAKK KLGIKIIYYI
     SPQIWAWKGK RIHLIKDCID KMAVIFPFEK TIYENAGVPV SFVGHPLVKK IAAAKDKHSG
     RTSLGLPLNE PIIALLPGSR HSEIERHIPI LVNTAKLLTL DNPKLRFVVP IAGTINPDKV
     KAYFSNQNLT VTFIQGQAIE CMSAADFVIV ASGTASLECA LLEKPMCIIY KSSFLTYVAA
     MYFIKVKFLG LCNLLANKMM VPEFLQYDCN AIELSRYISN FHNDPNQAKS MINQLAKLKE
     SLSSSQADCS LFDLVVAELP EKNA