ID   LPXB_ACTP7              Reviewed;         393 AA.
AC   B3GZJ7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=APP7_0007;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) 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; CP001091; ACE60659.1; -; Genomic_DNA.
DR   RefSeq; WP_012478271.1; NC_010939.1.
DR   AlphaFoldDB; B3GZJ7; -.
DR   SMR; B3GZJ7; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ACE60659; ACE60659; APP7_0007.
DR   KEGG; apa:APP7_0007; -.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   BioCyc; APLE537457:APP7_RS00035-MON; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001226; 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; Transferase.
FT   CHAIN           1..393
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000191457"
SQ   SEQUENCE   393 AA;  43880 MW;  EAA9F7279B6442ED CRC64;
     MIKKEAPLIA LVAGEISGDI LGAGLINALK LHYPNARFIG VAGPRMIQAG CETLFDMEEL
     AVMGLAEVVK HLPRLLKRRK QVIETMLAEK PDIFIGIDAP DFNLTVEEKL KASGIKTIHY
     VSPSVWAWRQ NRVQKIARAT NLVLAFLPFE KAFYDRFNVP CRFIGHTMAD AIALKPNRSE
     ACATLNLDET QRYLAILVGS RASEVRFLAE PFLKAAKILK QQYPDLQFLV PLVNDKRIAQ
     FEQIKAQVAP ELSVHILKGN ARQAMIAAEA SLLASGTAAL EGMLCKSPMV VGYKMKAMTY
     WLAKRLVKTK YISLPNLLAD EMLVPELIQD ECNPENLAWY LGNYLADDAD HRKQRNELKQ
     RFTELHKLIQ CDADAQAAQA VVDVLEANTS DQN