LOCUS       AJG08028.1               441 aa    PRT              BCT 08-APR-2015
DEFINITION  Escherichia coli ECC-1470 biofilm PGA synthase PgaCD,
            catalytic subunit protein.
ACCESSION   CP010344-1026
PROTEIN_ID  AJG08028.1
SOURCE      Escherichia coli ECC-1470
  ORGANISM  Escherichia coli ECC-1470
            Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
            Enterobacteriaceae; Escherichia.
REFERENCE   1  (bases 1 to 4803751)
  AUTHORS   Leimbach,A., Poehlein,A., Witten,A., Scheutz,F., Schukken,Y.,
            Daniel,R. and Dobrindt,U.
  TITLE     Complete Genome Sequences of Escherichia coli Strains 1303 and
            ECC-1470 Isolated from Bovine Mastitis
  JOURNAL   Genome Announc 3 (2) (2015)
   PUBMED   25814601
  REMARK    Publication Status: Online-Only
REFERENCE   2  (bases 1 to 4803751)
  AUTHORS   Leimbach,A., Poehlein,A., Daniel,R. and Dobrindt,U.
  TITLE     Direct Submission
  JOURNAL   Submitted (21-DEC-2014) Institute for Hygiene, University of
            Muenster, Mendelstrasse 7, Muenster, North Rhine-Westphalia 48149,
            Germany
COMMENT     Bacteria available from Dr. Ulrich Dobrindt, Institute of Hygiene,
            University of Muenster, email to: ulrich.dobrindt@ukmuenster.de.
            
            ##Genome-Assembly-Data-START##
            Assembly Method       :: Newbler v. 2.3; MIRA v. 3.4.0.1
            Genome Coverage       :: 88x
            Sequencing Technology :: Sanger; 454; Illumina
            ##Genome-Assembly-Data-END##
FEATURES             Qualifiers
     source          /organism="Escherichia coli ECC-1470"
                     /mol_type="genomic DNA"
                     /strain="ECC-1470"
                     /serotype="Ont:Hnt"
                     /isolation_source="udder persistent mastitis"
                     /host="Bos taurus (bovine)"
                     /db_xref="taxon:758831"
     protein         /gene="pgaC"
                     /locus_tag="E1470_c10690"
                     /note="poly-beta-1,6-N-acetyl-D-glucosamine synthase;
                     c-di-GMP-stimulated activity and dimerization"
                     /transl_table=11
BEGIN
        1 MINRIVSFFI LCLVLCIPLC VAYFHSGELM MRFVFFWPFF MSIMWIVGGV YFWVYRERHW
       61 PWGENAPAPQ LKDNPSISII IPCFNEEKNV EETIHAALAQ RYENIEVIAV NDGSTDKTRA
      121 ILDRMAAQIP HLRVIHLAQN QGKAIALKTG AAAAKSEYLV CIDGDALLDR DAAAYIVEPM
      181 LYNPRVGAVT GNPRIRTRST LVGKIQVGEY SSIIGLIKRT QRIYGNVFTV SGVIAAFRRS
      241 ALAEVGYWSD DMITEDIDIS WKLQLNQWTI FYEPRALCWI LMPETLKGLW KQRLRWAQGG
      301 AEVFLKNMTR LWRKENFRMW PLFFEYCLTT IWAFTCLVGF IIYAVQLAGV PLNIELTHIA
      361 ATHTAGILLC TLCLLQFIVS LMIENRYEHN LTSSLFWIIW FPVIFWMLSL ATTLVSFTRV
      421 MLMPKKQRAR WVSPDRGILR G
//