ID   LPXB_VIBPA              Reviewed;         379 AA.
AC   Q87MF0;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=VP2305;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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; BA000031; BAC60568.1; -; Genomic_DNA.
DR   RefSeq; NP_798684.1; NC_004603.1.
DR   RefSeq; WP_005480975.1; NC_004603.1.
DR   AlphaFoldDB; Q87MF0; -.
DR   SMR; Q87MF0; -.
DR   STRING; 223926.28807303; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; BAC60568; BAC60568; BAC60568.
DR   GeneID; 65555220; -.
DR   KEGG; vpa:VP2305; -.
DR   PATRIC; fig|223926.6.peg.2207; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002493; Chromosome 1.
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..379
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190189"
SQ   SEQUENCE   379 AA;  42764 MW;  0D40BFB14BA15E32 CRC64;
     MEKPLRIGII AGELSGDTLG EGFIKAVKER YPNAEFVGIG GPKMIAQGCE SLFDMEELAV
     MGLVEVLGRL PRLLKVKAEL VKYFTQNPPD VFVGIDAPDF NLRLELDLKQ AGIKTVHYVS
     PSVWAWRQKR IFKIEAATNL VLAFLPFEKA FYDKFNVPCE FIGHTLADAI PLQSEQAPAR
     DLLGLEQDKK WLAVLPGSRG SELKMLSQPF IETCKLLHQK YPGLGFVVAL VNQKRREQFE
     QAWKEHAPEL DFKLVDDTAR NVITASDAVM LASGTVALEC MLLKRPMVVG YRVNTFTAFL
     AKRLLKTKYV SLPNILADDE LVKEYLQDDC TPDNLFNEVS RLLESDNKPM LDKFTEMHHW
     IRKDADQQAA NAVLKLIEK