ID   LPXB_ALISL              Reviewed;         383 AA.
AC   B6EJW7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=VSAL_I2414;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(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; FM178379; CAQ80098.1; -; Genomic_DNA.
DR   RefSeq; WP_012550902.1; NC_011312.1.
DR   AlphaFoldDB; B6EJW7; -.
DR   SMR; B6EJW7; -.
DR   STRING; 316275.VSAL_I2414; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; CAQ80098; CAQ80098; VSAL_I2414.
DR   KEGG; vsa:VSAL_I2414; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001730; 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; Transferase.
FT   CHAIN           1..383
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000191458"
SQ   SEQUENCE   383 AA;  42929 MW;  1DEC4146FE77622D CRC64;
     MTKPLRIGIV AGELSGDTLG EGFIKSVKAQ YPNAEFVGIG GPKMIAQGCE SLFDMEELAV
     MGLVEVLGRL PRLLKVKAEL VRYFSQNPPD VFIGIDAPDF NLRLEKTLKD SGIKTVHYVS
     PSVWAWRPKR IFKIDAATDL VLAFLPFEKV FYDKYNVACE FIGHTLADAI PMQSDKIAAR
     KLLGLELDRQ WLAVLPGSRG GEVALIAKPF IETCQRIHQK HPNMGFVVAA VNEKRREQFE
     VIWKETAPEL KFIIIQDTAR NVMTAADSVL LASGTVALEC MLIKRPMVVG YQVNKLTGWI
     AQKLSITEFV SLPNVLAGKE LVQEFIQEEC HPDFLYPAME KVLSQDNSEL IDRFTEMHQW
     IKKDADKQAA NAVLRLINKE TAE