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LOCUS WP_000448391 323 aa linear BCT 17-JUN-2024 ACCESSION WP_000448391 VERSION WP_000448391.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR02208.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..323 /organism="Escherichia coli" /db_xref="taxon:562" gene 1..323 /gene="lpxM" /gene_synonym="msbB" Protein 1..323 /product="lauroyl-Kdo(2)-lipid IV(A) myristoyltransferase" /EC_number="2.3.1.243" /GO_component="GO:0009276 - Gram-negative-bacterium-type cell wall [Evidence IEA]" /GO_component="GO:0016020 - membrane [Evidence IEA]" /GO_function="GO:0016747 - acyltransferase activity, transferring groups other than amino-acyl groups [Evidence IEA]" /GO_process="GO:0009103 - lipopolysaccharide biosynthetic process [Evidence IEA]" /note="LpxM is lauroyl-Kdo(2)-lipid IV(A) myristoyltransferase, an enzyme characterized in Escherichia coli and involved in biosynthesis of the form of lipid A found in that species and some closely related species.; LpxM is lauroyl-Kdo(2)-lipid IV(A) myristoyltransferase, an enzyme characterized in Escherichia coli and involved in biosynthesis of the form of lipid A found in that species and some closely related species." /calculated_mol_wt=37245 Region 1..321 /region_name="PRK08943" /note="lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Validated" /db_xref="CDD:236355" Site order(139,142,144,161..164,210..212) /site_type="active" /note="putative acyl-acceptor binding pocket [active]" /db_xref="CDD:153246" ORIGIN 1 metkknnsey ipefdksfrh prywgawlgv aamagialtp pkfrdpilar lgriagrlgk 61 ssrrralinl slcfpersea ereaivdemf atapqamamm aelairgpek iqprvdwqgl 121 eiieemrrnn ekviflvphg wavdipamlm asqgqkmaam fhnqgnpvfd yvwntvrrrf 181 ggrlharndg ikpfiqsvrq gywgyylpdq dhgpehsefv dffatykatl paigrlmkvc 241 rarvvplfpi ydgkthrlti qvrppmddll eaddhtiarr mneeveifvg prpeqytwil 301 kllktrkpge iqpykrkdly pik