ID   LPXB_VIBVY              Reviewed;         380 AA.
AC   Q7MIH2;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=VV2544;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC95308.1; -; Genomic_DNA.
DR   RefSeq; WP_011079775.1; NC_005139.1.
DR   AlphaFoldDB; Q7MIH2; -.
DR   SMR; Q7MIH2; -.
DR   STRING; 672.VV93_v1c22630; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; BAC95308; BAC95308; BAC95308.
DR   KEGG; vvy:VV2544; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002675; Chromosome I.
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..380
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190191"
SQ   SEQUENCE   380 AA;  42610 MW;  FCF052209B276171 CRC64;
     MSNKPLRIGI VAGELSGDTL GEGFIKAIKA VHPDAEFVGI GGPKMIALGC QSLFDMEELA
     VMGLVEVLGR LPRLLKVKAE LVRYFTENPP DVFVGIDAPD FNLRLELDLK NAGIKTVHYV
     SPSVWAWRQK RIFKIAKATH LVLAFLPFEK AFYDKFNVPC EFIGHTLADA IPLESDKAPA
     RELLGLEQDK QWLAVLPGSR GSELKMLSQP FIETCKKLQQ AFPELGFVVA LVNQKRREQF
     EQAWKEYAPE LDFKLVDDTA RNVITASDAV MLASGTVALE CMLLKRPMVV GYRVNAVTAF
     LAKRLLKTQY VSLPNILADT ELVKEYLQDD CTPDNLFGEV SRLLEGDNHQ MLDKFTEMHH
     WIRKDADQQA ANAVLKLIEK