ID   LPXB_VIBCM              Reviewed;         379 AA.
AC   C3LQ19;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
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=VCM66_2170;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP001233; ACP06471.1; -; Genomic_DNA.
DR   RefSeq; WP_001081509.1; NC_012578.1.
DR   AlphaFoldDB; C3LQ19; -.
DR   SMR; C3LQ19; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; vcm:VCM66_2170; -.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001217; 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   NCBIfam; TIGR00215; lpxB; 1.
DR   PANTHER; PTHR30372; LIPID-A-DISACCHARIDE SYNTHASE; 1.
DR   PANTHER; PTHR30372:SF7; LIPID-A-DISACCHARIDE SYNTHASE; 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_1000191491"
SQ   SEQUENCE   379 AA;  42250 MW;  646808F3DDFA3CCE CRC64;
     MNRPLRIGIV VGELSGDTLG EGFIKAIRAR YPDAEFVGIG GPKMNALGCQ SLFDMEELAV
     MGLVEVLGRL PRLLKVKAEL VKYFTANPPD VFVGIDAPDF NLRLELSLKQ AGIKTVHYVS
     PSVWAWRQNR IHGIAAATHL VLAFLPFEKA FYDKFNVPCE FIGHTLADSI PLASDKLAAR
     QLLGLDEQRR WLAVLPGSRG SEMKMLAEPF IATCQKLQAR YPDLGFVVAL VNAKRRAQFE
     QAWQQVAPEL NFVLVDDTAR NVITAADAVM LASGTVALEC MLLKRPMVVG YRVNAFTAFL
     AKRLLKTPYV SLPNILAGEE LVKELLQDHC TVDNLYHEVS RLLESDNQAL MDKFTEMHQW
     IRKDADQQAA QAVLHLIQK
//