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colanic acid biosynthesis acetyltransferase WcaF [Escherichia


LOCUS       WP_001153566             182 aa            linear   BCT 25-JAN-2021
            coli].
ACCESSION   WP_001153566
VERSION     WP_001153566.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Scott,P.M., Erickson,K.M. and Troutman,J.M.
  TITLE     Identification of the Functional Roles of Six Key Proteins in the
            Biosynthesis of Enterobacteriaceae Colanic Acid
  JOURNAL   Biochemistry 58 (13), 1818-1830 (2019)
   PUBMED   30821147
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Zhang,J. and Poh,C.L.
  TITLE     Regulating exopolysaccharide gene wcaF allows control of
            Escherichia coli biofilm formation
  JOURNAL   Sci Rep 8 (1), 13127 (2018)
   PUBMED   30177768
  REMARK    Publication Status: Online-Only
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  :: BlastRule
            Evidence Accession :: NBR013811
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..182
                     /gene="wcaF"
     Protein         1..182
                     /product="colanic acid biosynthesis acetyltransferase
                     WcaF"
                     /calculated_mol_wt=19858
     Region          1..180
                     /region_name="WcaF"
                     /note="colanic acid biosynthesis acetyltransferase WcaF;
                     TIGR04008"
                     /db_xref="CDD:188523"
     Site            order(77,79,87,97,99,105,111..113,130,132,135,154,170)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:100063"
     Site            order(79,81,111,113,132,134..135,140,152..153,158..159,
                     168..169,171)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:100063"
     Site            order(79,81,111)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:100063"
     Site            order(111,113,132,134..135,140,150,152..153,158..159,166,
                     168..169,171,175)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:100063"
ORIGIN      
        1 mqdlsgfsvp kgfrggnaik vqlwwavqat ifawspqvly rwrafllrlf gakigknvvi
       61 rpsvkitypw kltlgdyvwv gddvnlytlg eitigahsvi sqksylctgs hdhasqhfti
      121 natpivigek cwlatdvfva pgvtigdgtv vgarssvfks lpanvvcrgn pavvirkrve
      181 te