LPXB_HELPH
ID LPXB_HELPH Reviewed; 360 AA.
AC Q1CT05;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=HPAG1_0850;
OS Helicobacter pylori (strain HPAG1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=357544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPAG1;
RX PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA Gordon J.I.;
RT "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT pylori strain: evolution during disease progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(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; CP000241; ABF84917.1; -; Genomic_DNA.
DR RefSeq; WP_001142220.1; NC_008086.1.
DR AlphaFoldDB; Q1CT05; -.
DR SMR; Q1CT05; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; ABF84917; ABF84917; HPAG1_0850.
DR KEGG; hpa:HPAG1_0850; -.
DR HOGENOM; CLU_036577_3_1_7; -.
DR OMA; PTVWAWR; -.
DR OrthoDB; 1258510at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000008835; 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_0000255188"
SQ SEQUENCE 360 AA; 41401 MW; ACDF02EC3B6FC745 CRC64;
MPTILVSALE ASSNIHLEEL RQNLPKDYRF IGVFEGKNAL YSPREFSIMG FRDVIGRLGF
LLKAHKEMVQ LAKQADMVLL MDSSSFNIPL AKKIKKQDPH KKIMYYILPQ VWAWKKWRAK
SLEKYCDFLG AILPFEVGYY QKKAQYVGHP LLDEIKYYKK DIKGETLVFM PGSRKSEIAK
IFPLFVKAAQ ILEQNEGFKR RVLVVPSFFK GLDLKALYGE DIELFEISYD AHKSLFEAEF
AFICSGTATL EAALIGTPFV LAYRAKTMDF LIARMLVNLH YIGLANIFYN ALNDETPGLG
ESQLHPELIQ HFLSVEGLLK AYEEMDRERY FKESLRLREY LASGSARKIA NEMAFLLNLT