ID   LPXB_PHOPR              Reviewed;         380 AA.
AC   Q6LN37;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=PBPRA2955;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR378672; CAG21289.1; -; Genomic_DNA.
DR   RefSeq; WP_011219556.1; NC_006370.1.
DR   AlphaFoldDB; Q6LN37; -.
DR   SMR; Q6LN37; -.
DR   STRING; 298386.PBPRA2955; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; ppr:PBPRA2955; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000593; 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   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: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; Reference proteome; Transferase.
FT   CHAIN           1..380
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255205"
SQ   SEQUENCE   380 AA;  42042 MW;  23475F77FE82EED9 CRC64;
     MTKPLRIGIV AGEISGDILG AGFIRAIKAQ YPDAEFVGVA GPRMEAEGCK ALFDMEELAV
     MGIVEVLGRL PRLLKVKAEL VKYFTENPPD VFVGIDAPDF NLRLELDLKQ HGIKTVHYVS
     PSVWAWRQKR IFKIEAATNL VLAFLPFEKA FYDKFNVPCE FVGHTMADAI PLETDKAAAQ
     ALLNLDGSKR WLAVLPGSRG SEMGMLAAPF IETCKLLKQK HPDLGFVVAL VNEKRREQFQ
     LAWQETAPEL DFVLVNDTAR NVMIASDAVL LASGTVALEC MLVGRPMVVG YKVKPLTAWI
     IRRLVKTKYV SLANILADKP LVTELLQEDC VPEKLSAEVD RILSSDNTEL LSEFSIMHQS
     IKCDADNRAA HAVLSLINKV
//