ID   LPXB_HELPJ              Reviewed;         360 AA.
AC   Q9ZKY2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Lipid-A-disaccharide synthase;
DE            EC=2.4.1.182;
GN   Name=lpxB; OrderedLocusNames=jhp_0801;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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}.
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DR   EMBL; AE001439; AAD06363.1; -; Genomic_DNA.
DR   PIR; D71888; D71888.
DR   RefSeq; WP_001142216.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZKY2; -.
DR   SMR; Q9ZKY2; -.
DR   STRING; 85963.jhp_0801; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; AAD06363; AAD06363; jhp_0801.
DR   KEGG; hpj:jhp_0801; -.
DR   PATRIC; fig|85963.30.peg.171; -.
DR   eggNOG; COG0763; Bacteria.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000804; 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..360
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190170"
SQ   SEQUENCE   360 AA;  41566 MW;  44A7504AC031BB2C CRC64;
     MPTILVSALE ASSNIHLEEL RHNLPKDYRF IGVFESKEAL YSPREFSIMG FRDVIGRLGF
     LLKAHKEMVQ LAKQADMVLL MDSSSFNIPL AKKIKKQDPH KKIMYYILPQ VWAWKKWRAK
     SLEKYCDFLG AILPFEVGYY QKKAQYVGHP LLDEIKYYKK DIKGETLVFM PGSRKSEIAK
     MFPLFVKAAQ ILEQNEGFKR RVLVVPSFFK GLDLKALYGE DIKLFEISYD AHKSLFEAEF
     AFICSGTATL EAALIGTPFA LAYRAKTMDF LIARMLVNLH YIGLANIFYN ALNNETPGLG
     ESQLHPELIQ HFLSVEGLLK AYEEMDRERY FKESLRLREY LKHGSARKIA EEMAFLLNLT