ID   LPXB_VIBC1              Reviewed;         379 AA.
AC   A7MY02;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   02-SEP-2026, 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};
GN   OrderedLocusNames=VIBHAR_03224;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) 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 + UDP + H(+);
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; CP000789; ABU72173.1; -; Genomic_DNA.
DR   RefSeq; WP_012128689.1; NC_009783.1.
DR   AlphaFoldDB; A7MY02; -.
DR   SMR; A7MY02; -.
DR   KEGG; vha:VIBHAR_03224; -.
DR   PATRIC; fig|338187.25.peg.2966; -.
DR   UniPathway; UPA00973; -.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005543; F:phospholipid binding; IEA:TreeGrafter.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01635; Glycosyltransferase_GTB-type; 1.
DR   HAMAP; MF_00392; LpxB; 1.
DR   InterPro; IPR003835; Glyco_trans_19.
DR   NCBIfam; TIGR00215; lpxB; 1.
DR   PANTHER; PTHR30372; LIPID-A-DISACCHARIDE SYNTHASE; 1.
DR   PANTHER; PTHR30372:SF4; LIPID-A-DISACCHARIDE SYNTHASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02684; LpxB; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Transferase.
FT   CHAIN           1..379
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000049425"
SQ   SEQUENCE   379 AA;  42782 MW;  D6ED1C97B9F9F932 CRC64;
     MERPLRIGII AGELSGDTLG EGFIKAVKQQ YPDAEFVGIG GPKMIAQGCE SLFDMEELAV
     MGLVEVLGRL PRLLKVKAQL VKYFTENPPD VFIGIDAPDF NLRVELDLKN AGIKTVHYVS
     PSVWAWRQKR IFKIEAATNL VLAFLPFEKA FYDKFNVPCE FIGHTLADAI PLQSDKASAR
     EILGLEQDKQ WLSVLPGSRG SELKMLSQPF IETCKKLHQK FPDIGFVVAL VNQKRREQFE
     QAWKEHAPEL DFKLVDDTAR NVITASDAVM LASGTVALEC MLLKRPMVVG YRVNAVTAFL
     AKRLLKTKYV SLPNILADTE LVKEYLQDDC TPDNLFDEVS RLLESDNREM LDKFTEMHHW
     IRKDADQQAA NAVLKLIEK
//