ID   LPXB_HELPY              Reviewed;         360 AA.
AC   O25537;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Lipid-A-disaccharide synthase;
DE            EC=2.4.1.182;
GN   Name=lpxB; OrderedLocusNames=HP_0867;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD07909.1; -; Genomic_DNA.
DR   PIR; C64628; C64628.
DR   RefSeq; NP_207661.1; NC_000915.1.
DR   RefSeq; WP_001142178.1; NC_018939.1.
DR   AlphaFoldDB; O25537; -.
DR   SMR; O25537; -.
DR   STRING; 85962.C694_04440; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PaxDb; O25537; -.
DR   EnsemblBacteria; AAD07909; AAD07909; HP_0867.
DR   KEGG; hpy:HP_0867; -.
DR   PATRIC; fig|85962.47.peg.921; -.
DR   eggNOG; COG0763; Bacteria.
DR   OMA; PTVWAWR; -.
DR   PhylomeDB; O25537; -.
DR   BioCyc; MetaCyc:HP_RS04230-MON; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000429; 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..360
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190169"
SQ   SEQUENCE   360 AA;  41518 MW;  420421646FCE067D CRC64;
     MPTILVSALE ASSNAHLEEL RQNLPEDYRF IGVFEGKEVL YSPREFSIMG FRDVIGRLGF
     LLKAHKEMVQ LAKQADMVLL MDSSSFNIPL AKKIKKQDPH KKIMYYILPQ VWAWKKWRAK
     SLEKYCDFLG AILPFEVGYY QKKAQYVGHP LLDEIKHYKK DIKGETLVFM PGSRKSEIAK
     MFPLFVKAAQ MLEQNEGFKR RVLVVPSFFK GLDLKALYGE DIQLFEISYD AHKSLFEAEF
     AFICSGTATL EAALIGTPFV LAYRAKTMDF LIARMLVNLH YIGLANIFYN ALNNETPGLG
     ESQLHPELIQ HFLSVEGLLK AYKEMDRERY FKESLRLREY LKHGSARKIA NEMAFLLNLT