ID   LPXB_RHOPA              Reviewed;         393 AA.
AC   Q6N5R2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=RPA2909;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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; BX572602; CAE28350.1; -; Genomic_DNA.
DR   RefSeq; WP_011158458.1; NC_005296.1.
DR   AlphaFoldDB; Q6N5R2; -.
DR   SMR; Q6N5R2; -.
DR   STRING; 258594.RPA2909; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PRIDE; Q6N5R2; -.
DR   EnsemblBacteria; CAE28350; CAE28350; RPA2909.
DR   GeneID; 66893991; -.
DR   KEGG; rpa:RPA2909; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_5; -.
DR   OMA; PTVWAWR; -.
DR   PhylomeDB; Q6N5R2; -.
DR   BioCyc; RPAL258594:TX73_RS14835-MON; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001426; 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..393
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255214"
SQ   SEQUENCE   393 AA;  42699 MW;  301A25B00E36408F CRC64;
     MSGAAKTGDR VRTVYLIATE ESGDRLGAAL MRELRARLGS KVRFAGVGGH CMAGEGLASL
     FPIEELSIIG FAAVVQRLPM ILKLIRRAVD AVLTAKPDIL VIIDSPDFTH RVARRVRQRD
     PSIPIVDYVS PTVWAWRPGR ARAMLGYVDH VLALLPFEPA EYRRLQGPPC SYVGHPLTEQ
     FGSLRPDAAE QARREASPPV LLVLPGSRRS EVRHHAAAFG DTLARLKHEG VAFEAVLPTT
     PHLEGLVRAA VASWEVQPRI VVGEQDKRAA FRIAHAALAK SGTVTLELAI AGVPMVTAYR
     AGSVEIWIAR RVVRPGTVIL ANLVMGDDVI PEFIQEDCVP DKLVPAVRDL LGNTPARRRQ
     LAGFAKIDDI LSTGEQTPSG RAADIVLDVM RHA