ID   LPXB_BURM1              Reviewed;         389 AA.
AC   A9AIM7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=Bmul_1270, BMULJ_01977;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-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 + 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; CP000868; ABX14958.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG43894.1; -; Genomic_DNA.
DR   RefSeq; WP_012213142.1; NC_010804.1.
DR   AlphaFoldDB; A9AIM7; -.
DR   SMR; A9AIM7; -.
DR   STRING; 395019.Bmul_1270; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; BAG43894; BAG43894; BMULJ_01977.
DR   KEGG; bmj:BMULJ_01977; -.
DR   KEGG; bmu:Bmul_1270; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_4; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000008815; Chromosome 1.
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..389
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000191466"
SQ   SEQUENCE   389 AA;  42378 MW;  81452B35002A1BA6 CRC64;
     MPLPTTQLRL AMVAGEPSGD LLAASLLGGL RERLPAPTHY YGIGGARMIA QGFDSHWQMD
     KLTVRGYVEA LGQIPEILRI RGELKRQLLA ERPDAFIGVD APDFNFNVEQ AARDAGIPSI
     HFVCPSIWAW RGGRIKKIAK SVDHMLCLFP FEPAILDKAG VASTYVGHPL ADEIPLEPDT
     HGARIALGLP ADGPVIAVLP GSRRSEIALI GPTFFAAMAL MQQREPGLRF VMPAATPALR
     ELLQPLVDAH PQLALTITDG RSQVAMTAAD AILVKSGTVT LEAALLKKPM VISYKVPWLT
     GQIMRRQGYL PYVGLPNILA GRFVVPELLQ HFATPEALAD ATLTQLRDDA NRRTLTEVFT
     EMHLSLRQNT AAKAAEAVAR VLDQRKRRA