ID   LPXB_HELPG              Reviewed;         360 AA.
AC   B5Z7M7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=HPG27_821;
OS   Helicobacter pylori (strain G27).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=563041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G27;
RX   PubMed=18952803; DOI=10.1128/jb.01416-08;
RA   Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA   Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT   "The complete genome sequence of Helicobacter pylori strain G27.";
RL   J. Bacteriol. 191:447-448(2009).
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; CP001173; ACI27576.1; -; Genomic_DNA.
DR   RefSeq; WP_001142235.1; NC_011333.1.
DR   AlphaFoldDB; B5Z7M7; -.
DR   SMR; B5Z7M7; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ACI27576; ACI27576; HPG27_821.
DR   KEGG; hpg:HPG27_821; -.
DR   HOGENOM; CLU_036577_3_1_7; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001735; 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_1000123052"
SQ   SEQUENCE   360 AA;  41582 MW;  10D61A19E0842462 CRC64;
     MPTILVSALE ASSNMHLEEL HRNLPEDYRF IGVFEGKNAL YSPREFSIMG FRDVIGRLGF
     LLKAHKEMVQ LAKQADMVLL MDSSSFNIPL AKKIKKQDPH KKIMYYILPQ VWAWKKWRAK
     SLEKYCDFLG AILPFEVGYY QKKAQYVGHP LLDEIKYYKK DIKGETLVFM PGSRKSEIAK
     MFPLFVKVAQ ILEQNEGFKR RVLVVPSFFK GLDLKALYGE DIQLFEISYD AHKSLFEAEF
     AFICSGTATL EAALIGTPFV LAYRAKTMDF LIARMLVNLH YIGLANIFYN ALNDETPGLG
     ESQLHPELIQ HFLSVEGLLK AYEEMDRERY FKESLRLREY LKHGSARKIA NEMAFLLNLT