LOCUS       APA96467.1               289 aa    PRT              BCT 30-JAN-2018
DEFINITION  Nocardia seriolae Lipase protein.
ACCESSION   CP017839-2376
PROTEIN_ID  APA96467.1
SOURCE      Nocardia seriolae
  ORGANISM  Nocardia seriolae
            Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
            Nocardiaceae; Nocardia.
REFERENCE   1  (bases 1 to 8304518)
  AUTHORS   Han,H.-J.
  TITLE     Genome sequence of Nocardia seriolae strain EM150506, isolated from
            Anguila japonica
  JOURNAL   Unpublished
REFERENCE   2  (bases 1 to 8304518)
  AUTHORS   Han,H.-J.
  TITLE     Direct Submission
  JOURNAL   Submitted (21-OCT-2016) Pathology Research Division, National
            Institute of Fisheries Science, #216, Gijanghaean-ro, Gijang-eup,
            Gijang-gun, Busan 46083, South Korea
COMMENT     DNA/bacteria available from National Institute of Fisheries Science
            (NIFS) in South Korea.
            
            ##Genome-Assembly-Data-START##
            Assembly Method       :: SMRT analysis v. 2.3.0
            Genome Coverage       :: 156x
            Sequencing Technology :: PacBio
            ##Genome-Assembly-Data-END##
FEATURES             Qualifiers
     source          /organism="Nocardia seriolae"
                     /mol_type="genomic DNA"
                     /strain="EM150506"
                     /host="Anguilla japonica"
                     /db_xref="taxon:37332"
                     /geo_loc_name="South Korea"
                     /collection_date="2015-05-06"
     protein         /locus_tag="NS506_02402"
                     /function="Disulfide bond; Hydrolase; Lipid degradation;
                     Lipid metabolism; Secreted; Serine esterase; Signal."
                     /note="Catalyzes the hydrolysis of p-nitrophenyl esters,
                     alpha- and beta-naphthyl esters, and triacylglycerols,
                     with a preference for medium acyl chain length (C8-C12).
                     Shows a much higher hydrolysis rate of glycerol esters of
                     unsaturated C16 and C18 fatty acids than that of their
                     saturated counterparts, and a preference for cis double
                     bond. Is also able to hydrolyze several natural oils and
                     Tween detergents. Also displays thioesterase and
                     phospholipase activities, towards palmitoyl-coenzyme A and
                     diheptanoyl glycerophosphocholine, respectively. Shows
                     transesterification activity of racemic 1-phenyl ethanol
                     with vinyl acetate in hexane, proceeding with partial (R)-
                     enantioselectivity; Belongs to the 'GDSL' lipolytic enzyme
                     family"
                     /transl_table=11
                     /db_xref="UniProtKB/Swiss-Prot:Q93MW7"
BEGIN
        1 MKLKHCLSTI AIVAAGTLVG IAPAGASGTK YVALGDSYAA GIGISNILDT TCSRSDRNYA
       61 HLFAAQRGYS LTDVTCGGAT TDSVTATQLS AVTSDTALVT LGVGGNDIGF GDIVKDCVMA
      121 GTLGTGSGTG SAVLQDLGTG STSGSAELLL GCKHKYDASM PTRLSQTSAK VAKLVSDIKS
      181 RAPQARVVLV GYPHILPDNA ALCAGRQPVL PGDVDWARDT VVGGLNTMLR SQAGTEYFST
      241 YEIYNGHDAC EAIPDRWVNG TSVDNGEGAR FHPNQYGHAA TAQQMVATL
//