ID   LPXB_CAMJE              Reviewed;         364 AA.
AC   Q9PIK8; Q0PBL8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Lipid-A-disaccharide synthase;
DE            EC=2.4.1.182;
GN   Name=lpxB; OrderedLocusNames=Cj0288c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL34441.1; -; Genomic_DNA.
DR   PIR; F81447; F81447.
DR   RefSeq; WP_002858730.1; NC_002163.1.
DR   RefSeq; YP_002343729.1; NC_002163.1.
DR   AlphaFoldDB; Q9PIK8; -.
DR   SMR; Q9PIK8; -.
DR   STRING; 192222.Cj0288c; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PaxDb; Q9PIK8; -.
DR   PRIDE; Q9PIK8; -.
DR   EnsemblBacteria; CAL34441; CAL34441; Cj0288c.
DR   GeneID; 904612; -.
DR   KEGG; cje:Cj0288c; -.
DR   PATRIC; fig|192222.6.peg.281; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_1_7; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000799; 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; Reference proteome; Transferase.
FT   CHAIN           1..364
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190156"
SQ   SEQUENCE   364 AA;  41581 MW;  53DA0DA1979A2C5F CRC64;
     MKTFLVCALE PSANLHLKEV LKAYKKDFGE FELHGIYDES LCKEFDLNSK PLYSSHEFSA
     MGFIEVLPLI FKAKKAIKEL ANLSFTQKIN GILCIDSPAF NIPFAKALKK AGSKIPRIYY
     ILPQVWAWKK GRIPIIESHF DILASILPFD NQFFNKSTYI GHPLLDEIKE FKNQEDINHT
     FSKKDDEKTI AFLPGSRRSE IRRLMPIFKE LSQKFKGKKI LCVPSFNLEK LEVYGDISEF
     KIESNTPKVL KKADFAFICS GTATLEAALV GTPFVLAYKA KAIDIFIAKL FVKLKHIGLA
     NIFCDFAGKE ALNPEFLQDK VNVLNLYEAY NKYDYKAFFA KVDFLKEYLQ FGSAKNLAKI
     LNEI