ID   LPXB_RHOCS              Reviewed;         401 AA.
AC   B6IST7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   02-SEP-2026, entry version 78.
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=RC1_1194;
OS   Rhodospirillum centenum (strain ATCC 51521 / SW).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodospirillales; Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=414684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW;
RA   Touchman J.W., Bauer C., Blankenship R.E.;
RT   "Genome sequence of Rhodospirillum centenum.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 + UDP + H(+);
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; CP000613; ACI98608.1; -; Genomic_DNA.
DR   RefSeq; WP_012566396.1; NC_011420.2.
DR   AlphaFoldDB; B6IST7; -.
DR   SMR; B6IST7; -.
DR   STRING; 414684.RC1_1194; -.
DR   KEGG; rce:RC1_1194; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_5; -.
DR   OrthoDB; 9801642at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001591; Chromosome.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005543; F:phospholipid binding; IEA:TreeGrafter.
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:SF4; LIPID-A-DISACCHARIDE SYNTHASE, MITOCHONDRIAL-RELATED; 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; Reference proteome; Transferase.
FT   CHAIN           1..401
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000205847"
SQ   SEQUENCE   401 AA;  43713 MW;  C25BE37E998BB01F CRC64;
     MKPLLIFLIA GEPSGDVLGG RLMAALREAM EGHVEFAGVG GPRMAEQGLQ SLFPMEDLAL
     FGLAELLPRL PTLLKRLDQT TKAVLERTPD AVVSIDAPDF CFRVEQRLRR AGARMPLIHY
     VAPTVWAWRP GRARKVAKFL DHLLALLPFE PPYFEAVGLP CTFVGHPVVE SGADAGDGER
     FRRRHGIAPD ATVLTVLPGS RRSEVTKLLP DFGATLEILA SRYPDLQVVV PTVPGVAETV
     AEAVQSWPVP AITLLGDADK YDAFAASTAA LAASGTVALE LALARVPAVI AYRIHPVSHA
     LYRRFIRVRY VNLVNIMLDR PLVPELLQQD CTPDRLALAV DRLLNEPSAR QEQIDGVTEV
     ARWLGQGDVP PSRRAAEAVL NVITKRVIAD RQGQTPGRSR S
//