ID   LPXB_HELAH              Reviewed;         360 AA.
AC   Q17WJ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
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};
GN   OrderedLocusNames=Hac_1230;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ99984.1; -; Genomic_DNA.
DR   RefSeq; WP_011578091.1; NC_008229.1.
DR   AlphaFoldDB; Q17WJ2; -.
DR   SMR; Q17WJ2; -.
DR   STRING; 382638.Hac_1230; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; hac:Hac_1230; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_1_7; -.
DR   OrthoDB; 9801642at2; -.
DR   BioCyc; HACI382638:HAC_RS05320-MONOMER; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000775; 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   NCBIfam; TIGR00215; lpxB; 1.
DR   PANTHER; PTHR30372; LIPID-A-DISACCHARIDE SYNTHASE; 1.
DR   PANTHER; PTHR30372:SF7; LIPID-A-DISACCHARIDE SYNTHASE; 1.
DR   Pfam; PF02684; LpxB; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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_1000049402"
SQ   SEQUENCE   360 AA;  41656 MW;  987155A926C94FEB CRC64;
     MPTILVSALE TSSNVHLEEL RRNLPKDYRF IGVFEGSGAL YSPREFSVMG FRDVIGRLGF
     LFKVYKEMIQ LAKQADMVLL MDSSSFNIPL AKKIKKQDSH KKIMYYILPQ VWAWKKWRAK
     TLEKYCDFLG AILPFEVSYY QKKAQYVGHP LLDEIKYYKK DIKGETLVFM PGSRKSEIAK
     IFPLFVEVAR ILEQNEGFKR RVLVVPSFFK GLDLKALYGE GIEWFEISYD AHKSLFEAEF
     AFICSGTATL EAALIGTPFV LAYRAKTMDF LIARMFVNLH YIGLANIFYN ALNDETPGLG
     ESQLHPELIQ HFLSVESLIR AYKDMDRERY FKESLKLREY LMHGSARKIA SEIAFLLNLT
//