ID   LPXB_NEIMF              Reviewed;         384 AA.
AC   A1KRN0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=NMC0191;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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; AM421808; CAM09508.1; -; Genomic_DNA.
DR   RefSeq; WP_002220209.1; NC_008767.1.
DR   AlphaFoldDB; A1KRN0; -.
DR   SMR; A1KRN0; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; CAM09508; CAM09508; NMC0191.
DR   KEGG; nmc:NMC0191; -.
DR   HOGENOM; CLU_036577_3_0_4; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002286; 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"
FT                   /id="PRO_1000049405"
SQ   SEQUENCE   384 AA;  42446 MW;  FBF9DE7A2ABA7A5F CRC64;
     MVDKKSPLIA VSVGEASGDL LGAHLIRAIR KRCPQARFVG IGGELMKAEG FESLYDQERL
     AVRGFAEVVR RLPEILRIRR GLVRDLLSLK PDVFVGIDAP DFNLGVAERL KRSGIPTVHY
     VSPSVWAWRR ERVGKIVHQV NRVLCLFPME PQLYLDAGGR AEFVGHPMAQ LMPLEDDRET
     ARKTLGVDAG IPVFALLPGS RVSEIDYMAP VFFQTALLLL ERYPAARFLL PAATEATKRR
     LAEVLQRPEF AGLPLTVIDR QSETVCRAAD AVLVTSGTAT LEVALCKRPM VISYKISPLT
     YAYVKRKIKV PHVGLPNILL GKEAVPELLQ SEAKPEKLAA ALADWYEHPD KVAALQQDFR
     ALHLLLKKDT ADLAARAVLE EAGC