ID   LPXB_NEIG1              Reviewed;         390 AA.
AC   Q5F5Y6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Lipid-A-disaccharide synthase {ECO:0000255|HAMAP-Rule:MF_00392};
DE            EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392};
GN   Name=lpxB {ECO:0000255|HAMAP-Rule:MF_00392}; OrderedLocusNames=NGO1782;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; AE004969; AAW90401.1; -; Genomic_DNA.
DR   RefSeq; WP_003689999.1; NC_002946.2.
DR   RefSeq; YP_208813.1; NC_002946.2.
DR   AlphaFoldDB; Q5F5Y6; -.
DR   SMR; Q5F5Y6; -.
DR   STRING; 242231.NGO_1782; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; AAW90401; AAW90401; NGO_1782.
DR   GeneID; 66754358; -.
DR   KEGG; ngo:NGO_1782; -.
DR   PATRIC; fig|242231.10.peg.2140; -.
DR   HOGENOM; CLU_036577_3_0_4; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000535; 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..390
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255200"
SQ   SEQUENCE   390 AA;  43064 MW;  8327E2A576E565BF CRC64;
     MWGQTNMVDK KSPLIAVSVG EASGDLLGAH LIRAIRKRCP QARLTGIGGE LMKAEGFESL
     YDQERLAVRG FVEVVRRLPE ILRIRRELVR DLLSLKPDVF VGIDAPDFNL GVAEKLKRAG
     IPTLHYVSPS VWAWRRERVG KIVHQVNRVL CLFPMEPQLY LDAGGRAEFV GHPMAQLMPL
     EDDRETARKT LGADVGIPVF ALLPGSRVSE IDYMAPVFFQ TALLLLERYP AARFLLPAAT
     EATKRRLAEV LQRPEFAGLA LTVTDRQSET VCRAADAVLV TSGTATLEVA LCKRPMVISY
     KISPLTYAYV KRKIKVPHVG LPNILLGKEA VPELLQSEAK PEKLAAALAD WYEHPDKVAA
     LQQDFGALHL LLKKDTADLA ARAVLEEAGC