phosphoethanolamine transferase [Escherichia coli].

LOCUS       WP_001054675             527 aa            linear   BCT 24-FEB-2020
ACCESSION   WP_001054675
VERSION     WP_001054675.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Bontemps-Gallo,S., Cogez,V., Robbe-Masselot,C., Quintard,K.,
            Dondeyne,J., Madec,E. and Lacroix,J.M.
  TITLE     Biosynthesis of osmoregulated periplasmic glucans in Escherichia
            coli: the phosphoethanolamine transferase is encoded by opgE
  JOURNAL   Biomed Res Int 2013, 371429 (2013)
   PUBMED   24228245
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 :: NBR011246
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..527
                     /gene="opgE"
     Protein         1..527
                     /product="phosphoethanolamine transferase"
                     /EC_number="2.7.-.-"
                     /calculated_mol_wt=59575
     Region          215..484
                     /region_name="LptA"
                     /note="Lipooligosaccharide Phosphoethanolamine Transferase
                     A (LptA) or Lipid A Phosphoethanolamine Transferase;
                     cd16017"
                     /db_xref="CDD:293741"
     Site            order(225,263,367,422..423,439)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293741"
     Site            order(225,263,367,423)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293741"
     Site            order(290,303,437,439..440)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293741"
ORIGIN      
        1 mnltlkeslv trsrvfspwt afyflqslli nlglgypfsl lytaaftail lllwrtlprv
       61 qkvlvgvssl vaacyfpfaq aygapnfntl lalhstnmee steiltifpw ysylvglfif
      121 algviairrk kenekarwnt fdslclvfsv atffvapvqn lawggvfklk dtgypvfrfa
      181 kdvivnnnev ieeqermakl sgmkdtwtvt avkpkyqtyv vvigesarrd algafgghwd
      241 ntpfassvng lifadyiaas gstqkslglt lnrvvdgkpq fqdnfvtlan ragfqtwwfs
      301 nqgqigeydt aiasiakrad evyflkegnf eadkntkdea lldmtaqvla qehsqpqliv
      361 lhlmgshpqa cdrtkgkyet fvqsketscy lytmtqtddl lrklydqlrn sgssfslvyf
      421 sdhglafker gkdvqylahd dkyqqnfqvp fmvissddka hrvikarrsa ndflgffsqw
      481 tgikakeini kypfisekka gpiyitnfql qkvdynhlgt difdpkp