P10441 (LPXB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipid-A-disaccharide synthase
EC=2.4.1.182

Gene names

Name:	lpxB
Synonyms:	pgsB
Ordered Locus Names:	b0182, JW0177

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. HAMAP-Rule MF_00392
Catalytic activity	UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate = UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. HAMAP-Rule MF_00392
Pathway	Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 5/6. HAMAP-Rule MF_00392
Sequence similarities	Belongs to the LpxB family.

Ontologies

Keywords
Biological process	Lipid A biosynthesis Lipid biosynthesis Lipid metabolism
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid A biosynthetic process Inferred from mutant phenotype PubMed 6370995. Source: EcoliWiki
Cellular_component	cytosol Inferred from direct assay PubMed 6370995. Source: EcoCyc extrinsic component of plasma membrane Inferred from direct assay PubMed 3049593. Source: EcoCyc
Molecular_function	lipid-A-disaccharide synthase activity Inferred from direct assay PubMed 6370995. Source: EcoliWiki phospholipid binding Inferred from direct assay PubMed 19883124. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
tufA	P0CE47	2	EBI-553692,EBI-301077

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 382	382	Lipid-A-disaccharide synthase HAMAP-Rule MF_00392		PRO_0000190164
Experimental info
	Sequence conflict	149	1	F → V Ref.1
	Sequence conflict	149	1	F → V Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P10441 [UniParc]. Last modified July 19, 2003. Version 2. Checksum: 12C76B6ECA438B47	FASTA	382	42,382
	10 20 30 40 50 60 MTEQRPLTIA LVAGETSGDI LGAGLIRALK EHVPNARFVG VAGPRMQAEG CEAWYEMEEL 70 80 90 100 110 120 AVMGIVEVLG RLRRLLHIRA DLTKRFGELK PDVFVGIDAP DFNITLEGNL KKQGIKTIHY 130 140 150 160 170 180 VSPSVWAWRQ KRVFKIGRAT DLVLAFLPFE KAFYDKYNVP CRFIGHTMAD AMPLDPDKNA 190 200 210 220 230 240 ARDVLGIPHD AHCLALLPGS RGAEVEMLSA DFLKTAQLLR QTYPDLEIVV PLVNAKRREQ 250 260 270 280 290 300 FERIKAEVAP DLSVHLLDGM GREAMVASDA ALLASGTAAL ECMLAKCPMV VGYRMKPFTF 310 320 330 340 350 360 WLAKRLVKTD YVSLPNLLAG RELVKELLQE ECEPQKLAAA LLPLLANGKT SHAMHDTFRE 370 380 LHQQIRCNAD EQAAQAVLEL AQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the Escherichia coli gene for lipid A disaccharide synthase." Crowell D.N., Reznikoff W.S., Raetz C.R.H. J. Bacteriol. 169:5727-5734(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 149. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"First committed step of lipid A biosynthesis in Escherichia coli: sequence of the lpxA gene." Coleman J., Raetz C.R.H. J. Bacteriol. 170:1268-1274(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
[7]	"Sequence analysis of the Escherichia coli dnaE gene." Tomasiewicz H.G., McHenry C.S. J. Bacteriol. 169:5735-5744(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 329-382.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M19334 Genomic DNA. Translation: AAC36919.1. U70214 Genomic DNA. Translation: AAB08611.1. U00096 Genomic DNA. Translation: AAC73293.1. AP009048 Genomic DNA. Translation: BAA77857.2.
PIR	SYECLA. F64742.
RefSeq	NP_414724.1. NC_000913.3. YP_488484.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P10441.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
DIP	DIP-10122N.
IntAct	P10441. 19 interactions.
MINT	MINT-1246245.
STRING	511145.b0182.
Protein family/group databases
CAZy	GT19. Glycosyltransferase Family 19.
Proteomic databases
PaxDb	P10441.
PRIDE	P10441.
Protocols and materials databases
DNASU	944838.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73293; AAC73293; b0182. BAA77857; BAA77857; BAA77857.
GeneID	12931876. 944838.
KEGG	ecj:Y75_p0178. eco:b0182.
PATRIC	32115475. VBIEscCol129921_0189.
Organism-specific databases
EchoBASE	EB0541.
EcoGene	EG10546. lpxB.
Phylogenomic databases
eggNOG	COG0763.
HOGENOM	HOG000018003.
KO	K00748.
OMA	YIAPQEW.
OrthoDB	EOG6FBWZR.
ProtClustDB	PRK00025.
Enzyme and pathway databases
BioCyc	EcoCyc:LIPIDADISACCHARIDESYNTH-MONOMER. ECOL316407:JW0177-MONOMER. MetaCyc:LIPIDADISACCHARIDESYNTH-MONOMER.
UniPathway	UPA00359; UER00481.
Gene expression databases
Genevestigator	P10441.
Family and domain databases
HAMAP	MF_00392. LpxB.
InterPro	IPR003835. Glyco_trans_19. [Graphical view]
Pfam	PF02684. LpxB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00215. lpxB. 1 hit.
ProtoNet	Search...
Other
PRO	P10441.

Entry information

Entry name

LPXB_ECOLI

Accession

Primary (citable) accession number: P10441
Secondary accession number(s): P78298

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 19, 2003
Last modified:	February 19, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program