ID   LPXB_XANC8              Reviewed;         438 AA.
AC   Q4USP7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 74.
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=XC_2878;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAY49926.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000050; AAY49926.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_029629001.1; NC_007086.1.
DR   AlphaFoldDB; Q4USP7; -.
DR   SMR; Q4USP7; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; AAY49926; AAY49926; XC_2878.
DR   KEGG; xcb:XC_2878; -.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000420; 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..438
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255232"
SQ   SEQUENCE   438 AA;  47373 MW;  57F54210F9AF7125 CRC64;
     MTGIGNREPE HGAGAHVGAA VSVPDAASIP HSPLPIPGAR MRAPRIALIA GEASGDILGA
     GLIDALRRRY PDAEFVGIGG DAMRSAGCQT WFDASELAVM GLTEVLRHLP RLLKLRSAFR
     ERVLAWKPDV FIGIDAPDFN LPVERWLKQR GVRTVHYVSP SVWAWREKRA EKIGVSADLV
     LCLFPMEPPI YAKHGVDARF VGHPMADAIA YQADREAARA KLGLSTSSTV LAVLPGSRHG
     EISRLGDTFF QAAWLVSEHL PNLHVLVPAA NPGCKQLLAE QLSRSSLPVM RSHLLDGQAR
     TAMLAADVVL LASGTATLEA MLVKRPMVVG YKVAPLTYRI VKTLGLLKVN RYALPNILAN
     EDLAPELMQD DCTPERLCEA LLDWFKHPEK VAGLQSRYLA LHAQLRQDAS ARAAEAVAEL
     LTQRELGIGN RESGGAGS