ID   LPXB_PSEAB              Reviewed;         378 AA.
AC   Q02RB5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=PA14_17220;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(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; CP000438; ABJ12876.1; -; Genomic_DNA.
DR   RefSeq; WP_003109334.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02RB5; -.
DR   SMR; Q02RB5; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; pau:PA14_17220; -.
DR   PseudoCAP; PA14_17220; -.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   BioCyc; PAER208963:G1G74-1418-MONOMER; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000653; 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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
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..378
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000049408"
SQ   SEQUENCE   378 AA;  41280 MW;  46CEEEA4863C68B7 CRC64;
     MADGLRVALV AGEASGDILG SGLMQALRAR HPDIEFIGVG GPRMEAEGLS SYFPMERLSV
     MGLVEVLGRL PELLRRRKRL IRTLIEARPD VMIGIDAPDF TLGVEHKLRQ AGLRTVHYVS
     PSVWAWRQKR VLKIREACDL MLALFPFEAR FYEEHGVPVR FVGHPLANTI PLQADRAAAR
     ARLGLPADGQ VVALMPGSRG GEVGKLGALF LDTAQRLLVE RPGLRFVLPC ASAARREQIE
     QMLQGREPLP LTLLDGASHE ALAACDAVLI ASGTATLEAL LYKRPMVVAY RVAGLTYRIL
     KRLVKSPYIS LPNLLAGRLL VPELIQDAAT PQALAATLSP LLDDGSQQVE FFDAIHRALR
     QDASAQAAEA VLQLVERR
//