LPXB_ECOLI
ID LPXB_ECOLI Reviewed; 382 AA.
AC P10441; P78298;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Lipid-A-disaccharide synthase;
DE EC=2.4.1.182 {ECO:0000269|PubMed:6370995};
GN Name=lpxB; Synonyms=pgsB; OrderedLocusNames=b0182, JW0177;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2824445; DOI=10.1128/jb.169.12.5727-5734.1987;
RA Crowell D.N., Reznikoff W.S., Raetz C.R.H.;
RT "Nucleotide sequence of the Escherichia coli gene for lipid A disaccharide
RT synthase.";
RL J. Bacteriol. 169:5727-5734(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 149.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RX PubMed=3277952; DOI=10.1128/jb.170.3.1268-1274.1988;
RA Coleman J., Raetz C.R.H.;
RT "First committed step of lipid A biosynthesis in Escherichia coli: sequence
RT of the lpxA gene.";
RL J. Bacteriol. 170:1268-1274(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 329-382.
RX PubMed=3316192; DOI=10.1128/jb.169.12.5735-5744.1987;
RA Tomasiewicz H.G., McHenry C.S.;
RT "Sequence analysis of the Escherichia coli dnaE gene.";
RL J. Bacteriol. 169:5735-5744(1987).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=6370995; DOI=10.1016/s0021-9258(17)42924-3;
RA Ray B.L., Painter G., Raetz C.R.;
RT "The biosynthesis of gram-negative endotoxin. Formation of lipid A
RT disaccharides from monosaccharide precursors in extracts of Escherichia
RT coli.";
RL J. Biol. Chem. 259:4852-4859(1984).
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 -!- 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:0000269|PubMed:6370995};
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:0000269|PubMed:6370995};
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.
CC -!- INTERACTION:
CC P10441; P0CE47: tufA; NbExp=3; IntAct=EBI-553692, EBI-301077;
CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000305}.
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DR EMBL; M19334; AAC36919.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08611.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73293.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77857.2; -; Genomic_DNA.
DR PIR; F64742; SYECLA.
DR RefSeq; NP_414724.1; NC_000913.3.
DR RefSeq; WP_000139654.1; NZ_SSZK01000004.1.
DR PDB; 5W8N; X-ray; 2.02 A; A=1-382.
DR PDB; 5W8S; X-ray; 2.10 A; A=1-382.
DR PDB; 5W8X; X-ray; 1.98 A; A=1-382.
DR PDBsum; 5W8N; -.
DR PDBsum; 5W8S; -.
DR PDBsum; 5W8X; -.
DR AlphaFoldDB; P10441; -.
DR SMR; P10441; -.
DR BioGRID; 4260870; 581.
DR BioGRID; 849238; 6.
DR DIP; DIP-10122N; -.
DR IntAct; P10441; 26.
DR STRING; 511145.b0182; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR jPOST; P10441; -.
DR PaxDb; P10441; -.
DR PRIDE; P10441; -.
DR DNASU; 944838; -.
DR EnsemblBacteria; AAC73293; AAC73293; b0182.
DR EnsemblBacteria; BAA77857; BAA77857; BAA77857.
DR GeneID; 944838; -.
DR KEGG; ecj:JW0177; -.
DR KEGG; eco:b0182; -.
DR PATRIC; fig|1411691.4.peg.2097; -.
DR EchoBASE; EB0541; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_0_6; -.
DR InParanoid; P10441; -.
DR OMA; PTVWAWR; -.
DR PhylomeDB; P10441; -.
DR BioCyc; EcoCyc:LIPIDADISACCHARIDESYNTH-MON; -.
DR BioCyc; MetaCyc:LIPIDADISACCHARIDESYNTH-MON; -.
DR BRENDA; 2.4.1.182; 2026.
DR SABIO-RK; P10441; -.
DR UniPathway; UPA00359; UER00481.
DR PRO; PR:P10441; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IDA:EcoCyc.
DR GO; GO:0005543; F:phospholipid binding; IDA:EcoliWiki.
DR GO; GO:0009245; P:lipid A biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..382
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_0000190164"
FT CONFLICT 149
FT /note="F -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 16..32
FT /evidence="ECO:0007829|PDB:5W8X"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:5W8X"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:5W8X"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:5W8X"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:5W8X"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:5W8X"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:5W8X"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:5W8X"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:5W8X"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 202..222
FT /evidence="ECO:0007829|PDB:5W8X"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:5W8X"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:5W8X"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 277..284
FT /evidence="ECO:0007829|PDB:5W8X"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 334..345
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 349..364
FT /evidence="ECO:0007829|PDB:5W8X"
FT HELIX 369..380
FT /evidence="ECO:0007829|PDB:5W8X"
SQ SEQUENCE 382 AA; 42382 MW; 12C76B6ECA438B47 CRC64;
MTEQRPLTIA LVAGETSGDI LGAGLIRALK EHVPNARFVG VAGPRMQAEG CEAWYEMEEL
AVMGIVEVLG RLRRLLHIRA DLTKRFGELK PDVFVGIDAP DFNITLEGNL KKQGIKTIHY
VSPSVWAWRQ KRVFKIGRAT DLVLAFLPFE KAFYDKYNVP CRFIGHTMAD AMPLDPDKNA
ARDVLGIPHD AHCLALLPGS RGAEVEMLSA DFLKTAQLLR QTYPDLEIVV PLVNAKRREQ
FERIKAEVAP DLSVHLLDGM GREAMVASDA ALLASGTAAL ECMLAKCPMV VGYRMKPFTF
WLAKRLVKTD YVSLPNLLAG RELVKELLQE ECEPQKLAAA LLPLLANGKT SHAMHDTFRE
LHQQIRCNAD EQAAQAVLEL AQ
