ID   LPXB_SALTY              Reviewed;         382 AA.
AC   Q8ZRN9;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, 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}; OrderedLocusNames=STM0229;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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=2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl
CC         1-phosphate + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-
CC         glucosamine = H(+) + lipid A disaccharide (E. coli) + UDP;
CC         Xref=Rhea:RHEA:22668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57957,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58466, ChEBI:CHEBI:78847;
CC         Evidence={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: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC       from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC       acetyl-alpha-D-glucosamine: step 5/6. {ECO:0000255|HAMAP-
CC       Rule:MF_00392}.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00392}.
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DR   EMBL; AE006468; AAL19193.1; -; Genomic_DNA.
DR   RefSeq; NP_459234.1; NC_003197.2.
DR   RefSeq; WP_000741212.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZRN9; -.
DR   SMR; Q8ZRN9; -.
DR   STRING; 99287.STM0229; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PaxDb; Q8ZRN9; -.
DR   EnsemblBacteria; AAL19193; AAL19193; STM0229.
DR   GeneID; 1251747; -.
DR   KEGG; stm:STM0229; -.
DR   PATRIC; fig|99287.12.peg.242; -.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   PhylomeDB; Q8ZRN9; -.
DR   BioCyc; SENT99287:STM0229-MON; -.
DR   UniPathway; UPA00359; UER00481.
DR   Proteomes; UP000001014; Chromosome.
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..382
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190184"
SQ   SEQUENCE   382 AA;  42452 MW;  D84FB7284794CC59 CRC64;
     MAAQRPLTIA LVAGETSGDI LGAGLIRALK ARVPNARFVG VAGPRMQAEG CEAWYEMEEL
     AVMGIVEVLG RLRRLLHIRA DLTRRFTELK PDVFVGIDAP DFNITLEGNL KKKGIKTIHY
     VSPSVWAWRQ KRVFKIGRST HMVLAFLPFE KAFYDKFNVP CRFIGHTMAD AMPLDPDKNA
     ARDVLGIPHD AHCLALLPGS RGAEVEMLSA DFLKTAQLLR QRYPDLEVVV PLVNAKRREQ
     FEKIKAEVAP DLAVHLLDGM AREAMIASDA ALLASGTAAL ECMLAKCPMV VGYRMKPFTF
     WLAKRLVKTE YVSLPNLLAG RELVKELLQE ECEPQKLAEA LLPLLANGKT SHAMHDTFRE
     LHQQIRCNAD EQAADAVLEL AQ