ID   LPXB_GRABC              Reviewed;         393 AA.
AC   Q0BS63;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=GbCGDNIH1_1441;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000394; ABI62339.1; -; Genomic_DNA.
DR   RefSeq; WP_011632143.1; NC_008343.2.
DR   AlphaFoldDB; Q0BS63; -.
DR   SMR; Q0BS63; -.
DR   STRING; 391165.GbCGDNIH1_1441; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; gbe:GbCGDNIH1_1441; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_5; -.
DR   OrthoDB; 9801642at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001963; 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   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..393
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000072224"
SQ   SEQUENCE   393 AA;  42932 MW;  D2588B438EDED191 CRC64;
     MTAPLIYIVA GEHSGDVLGA RLIHALRAIN PSIRFAGIGG PRMEECGFQS LFPMHELAVM
     GLIEILPRVL KLRRRLQQTV QDIETRRPDL VLTIDSPGFC LRLLRAIQPF GIKRVHYVAP
     QVWAWREHRV KRFPGLWERM LCLLPFEEKW FAERNVPGQF VGHPVLESGA DQGDAARFRA
     RHSLADNARV IVLMPGSRAN EAGRLLPVYG ETLRLLMQNI PTITPVIPLA SSTAHTVRGA
     VSSWPVQPIF ITDIADKHDA FAAAEAALTK SGTSTLELAM GGVPMAVTYR VNRITAMMAR
     RLIRVPYVAM VNLLAGREIV PELLQENCTP TKIAAVLTSL MNNAPDTNGM GAADSQKQAL
     KAVVASLHAP NRHASDGLPS SAAAASIMEV LGQ
//