ID   LPXB_NEIMB              Reviewed;         384 AA.
AC   Q9K1F5;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Lipid-A-disaccharide synthase;
DE            EC=2.4.1.182;
GN   Name=lpxB; OrderedLocusNames=NMB0199;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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. {ECO:0000250}.
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;
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF40656.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE002098; AAF40656.1; ALT_INIT; Genomic_DNA.
DR   PIR; A81226; A81226.
DR   RefSeq; NP_273257.1; NC_003112.2.
DR   AlphaFoldDB; Q9K1F5; -.
DR   SMR; Q9K1F5; -.
DR   STRING; 122586.NMB0199; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PaxDb; Q9K1F5; -.
DR   EnsemblBacteria; AAF40656; AAF40656; NMB0199.
DR   KEGG; nme:NMB0199; -.
DR   PATRIC; fig|122586.8.peg.249; -.
DR   HOGENOM; CLU_036577_3_0_4; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
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"
FT                   /id="PRO_0000190172"
SQ   SEQUENCE   384 AA;  42420 MW;  0951D9F9BE00821D CRC64;
     MADKKSPLIA VSVGEASGDL LGAHLIRAIR KRCPQARFTG IGGELMKAEG FESLYDQERL
     AVRGFVEVVR RLPEILRIRR GLVRDLLSLK PDVFVGIDAP DFNLGVAEKL KRSGIPTVHY
     VSPSVWAWRR ERVGKIVHQV NRVLCLFPME PQLYLDAGGR AEFVGHPMAQ LMPLEDDRET
     ARQTLGVDAG IPVFALLPGS RVSEIDYMAP VFFQTALLLL ERYPAARFLL PAATEATKRR
     LAEVLQRPEF AGLPLTVIDR QSETVCRAAD AVLVTSGTAT LEVALCKRPM VISYKISPLT
     YAYVKRKIKV PHVGLPNILL GKEAVPELLQ SEAKPEKLAA ALADWYEHPD KVAALQQDFR
     ALHLLLKKDT ADLAARAVLE EAGC