ID   LPXB_VIBCH              Reviewed;         379 AA.
AC   Q9KPW5;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Lipid-A-disaccharide synthase;
DE            EC=2.4.1.182;
GN   Name=lpxB; OrderedLocusNames=VC_2247;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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. {ECO:0000250}.
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;
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE003852; AAF95391.1; -; Genomic_DNA.
DR   PIR; A82101; A82101.
DR   RefSeq; NP_231878.1; NC_002505.1.
DR   RefSeq; WP_001081509.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KPW5; -.
DR   SMR; Q9KPW5; -.
DR   STRING; 243277.VC_2247; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   DNASU; 2613169; -.
DR   EnsemblBacteria; AAF95391; AAF95391; VC_2247.
DR   GeneID; 57740870; -.
DR   KEGG; vch:VC_2247; -.
DR   PATRIC; fig|243277.26.peg.2143; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   BioCyc; VCHO:VC2247-MON; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
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_0000190188"
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