ID   LPXB_ALIF1              Reviewed;         383 AA.
AC   Q5E3F2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=VF_1949;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(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}.
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DR   EMBL; CP000020; AAW86444.1; -; Genomic_DNA.
DR   RefSeq; WP_011262425.1; NC_006840.2.
DR   RefSeq; YP_205332.1; NC_006840.2.
DR   AlphaFoldDB; Q5E3F2; -.
DR   SMR; Q5E3F2; -.
DR   STRING; 312309.VF_1949; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; AAW86444; AAW86444; VF_1949.
DR   KEGG; vfi:VF_1949; -.
DR   PATRIC; fig|312309.11.peg.1976; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000537; 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..383
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255231"
SQ   SEQUENCE   383 AA;  42958 MW;  13B1974E02CA9BD7 CRC64;
     MTKPLRIGIV AGELSGDTLG EGFIKSIKAQ YPDAEFVGIG GPKMIAQGCD SLFDMEELAV
     MGLVEVLGRL PRLLKVKAEL VRYFTQNPPD VFIGIDAPDF NLRLEKTLKD NGIKTVHYVS
     PSVWAWRPKR IFKIDAATDL VLAFLPFEKA FYDKYNVACE FIGHTLADAI PMETDKIAAR
     DLLGLEQERE WLAVLPGSRG GEVALIAKPF IETCQRIHKQ HPNMGFVVAA VNEKRREQFE
     TIWKATAPEL DFVIIQDTAR NVMTAADAVL LASGTVALEC MLVKRPMVVG YQVNKLTGWI
     AQKLSITEFV SLPNVLAGKE LVQEFIQEEC HPDFLYPAME KVLNNDNREL IEKFTEMHQW
     IRKDADKQAA NAVLRLINKE TAE