ID   LPXB_GLAP5              Reviewed;         387 AA.
AC   B8F5I8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=HAPS_0965;
OS   Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Glaesserella.
OX   NCBI_TaxID=557723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH0165;
RX   PubMed=19074396; DOI=10.1128/jb.01682-08;
RA   Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA   Jin M., Jin Q., Chen H.;
RT   "Complete genome sequence of Haemophilus parasuis SH0165.";
RL   J. Bacteriol. 191:1359-1360(2009).
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; CP001321; ACL32590.1; -; Genomic_DNA.
DR   RefSeq; WP_015939546.1; NC_011852.1.
DR   AlphaFoldDB; B8F5I8; -.
DR   SMR; B8F5I8; -.
DR   STRING; 557723.HAPS_0965; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ACL32590; ACL32590; HAPS_0965.
DR   KEGG; hap:HAPS_0965; -.
DR   PATRIC; fig|557723.8.peg.965; -.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000006743; 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; Reference proteome; Transferase.
FT   CHAIN           1..387
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000191487"
SQ   SEQUENCE   387 AA;  43061 MW;  AB11AC476A679460 CRC64;
     MTTSSPLIAI VAGEISGDIL GAGLIKALKV HYPNARFIGV AGEKMLKEGC ETLFDMEKLA
     VMGLAEVVRH LPRLLKRRKQ VIDTMLALKP DIFIGIDAPD FNLGVEEKLK AQGIKTIHYV
     SPSVWAWRQN RVHKIASATD LVLAFLPFEK AFYDRFNVPC RFIGHTMADA IALQPNRQEA
     CRLLQLDENQ HYVAILVGSR GSEVNFLSEP FLKTAQLLKA QYPDVQFLVP LVNEKRREQF
     EAIKAQVAPE LEVITLAGNA RAAMMVAEAT LLASGTAALE AMLCKSPMVV GYKMKPLTYW
     LAKRLVKTDY ISLPNLLANE PLVPELIQAD CSPENLAKHL SLYLSQMPED VAKKNALKQR
     FMELHQYIQC DADAQAAQAV VDVLNRE