lauroyl-Kdo(2)-lipid IV(A) myristoyltransferase [Vibrio

LOCUS       WP_008075783             321 aa            linear   BCT 17-JUN-2024
            sinaloensis].
ACCESSION   WP_008075783
VERSION     WP_008075783.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinaloensis
  ORGANISM  Vibrio sinaloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio oreintalis group.
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..321
                     /organism="Vibrio sinaloensis"
                     /db_xref="taxon:379097"
     gene            1..321
                     /gene="lpxM"
                     /gene_synonym="msbB"
     Protein         1..321
                     /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=36686
     Region          5..315
                     /region_name="LPLAT"
                     /note="Lysophospholipid acyltransferases (LPLATs) of
                     glycerophospholipid biosynthesis; cl17185"
                     /db_xref="CDD:473073"
     Site            order(142,145,147,164..167,213..215)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153246"
ORIGIN      
        1 mskprndfdp kaynptfewg flapkywgtw lgvfaslpls llpvkahnwi ahqiasrlvn
       61 krkgavhnir vnlslcfpek seqereqlvy qtlltagvfm mrfglltlrs sqwlqsqctl
      121 inehhltdct sqdenvillv phswsidipa vllaskglpv samakrqknp vsdwlmhrqr
      181 vqyggrvyer sggikpfiks ikegylgyyl pdqdhgaels efvdffattk atlpgltkla
      241 klskskiipt fasidphtgq ysiefmppie lqdseladar gmneaieyfv akepnqymwi
      301 lrllrtqqdg rnlyremrdk q