ID   LPXB_ACTP2              Reviewed;         393 AA.
AC   A3MY79;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=APL_0007;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN73115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MY79; -.
DR   SMR; A3MY79; -.
DR   STRING; 416269.APL_0007; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ABN73115; ABN73115; APL_0007.
DR   KEGG; apl:APL_0007; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001432; 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   CDD; cd01635; Glycosyltransferase_GTB-type; 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; Reference proteome; Transferase.
FT   CHAIN           1..393
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000049381"
SQ   SEQUENCE   393 AA;  43749 MW;  1975B14EBD68282E CRC64;
     MMTKEAPLIA LVAGEISGDI LGAGLINALK LHYPNARFIG VAGPRMIQAG CETLFDMEEL
     AVMGLAEVVK HLPRLLKRRK QVIETMLAEK PDIFIGIDAP DFNLTVEEKL KASGIKTIHY
     VSPSVWAWRQ NRVHKIARAT NLVLAFLPFE KAFYDRFNVP CRFIGHTMAD TIALKPNRAE
     ACVGLNLDEA QRYLAILVGS RASEVGFLAE PFLKAAQILK QQYPDLQFLV PLVNDKRIAQ
     FEQIKAQVAP ELSVHILKGN ARQAMIAAEA SLLASGTAAL EGMLCKSPMV VGYKMKAMTY
     WLAKRLVKTK YISLPNLLAD EMLVPELIQD ECNPENLAWY LGNYLADDAD HRKQRNELKQ
     RFTELHKLIQ CDADAQAAQA VVDVLEANTS DQN
//