LPXB_SALNS
ID LPXB_SALNS Reviewed; 382 AA.
AC B4SV11;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=SNSL254_A0251;
OS Salmonella newport (strain SL254).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=423368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL254;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001113; ACF62083.1; -; Genomic_DNA.
DR RefSeq; WP_000741216.1; NZ_CCMR01000003.1.
DR AlphaFoldDB; B4SV11; -.
DR SMR; B4SV11; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; ACF62083; ACF62083; SNSL254_A0251.
DR KEGG; see:SNSL254_A0251; -.
DR HOGENOM; CLU_036577_3_0_6; -.
DR OMA; PTVWAWR; -.
DR UniPathway; UPA00359; UER00481.
DR Proteomes; UP000008824; Chromosome.
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..382
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_1000123062"
SQ SEQUENCE 382 AA; 42452 MW; D844CCF247939FE3 CRC64;
MAAQRPLTIA LVAGETSGDI LGAGLIRALK ARVPNARFVG VAGPRMQAEG CEAWYEMEEL
AVMGIVEVLG RLRRLLHIRA DLTRRFTELK PDVFVGIDAP DFNITLEGNL KKQGIKTIHY
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
