endolysin [Staphylococcus phage phiETA].

FASTA View on NCBI
LOCUS       NP_510959                470 aa            linear   PHG 11-JAN-2023
ACCESSION   NP_510959
VERSION     NP_510959.1
DBLINK      BioProject: PRJNA485481
DBSOURCE    REFSEQ: accession NC_003288.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus phage phiETA
  ORGANISM  Staphylococcus phage phiETA
            Viruses; Duplodnaviria; Heunggongvirae; Uroviricota;
            Caudoviricetes; Azeredovirinae; Phietavirus; Phietavirus ETA.
REFERENCE   1
  AUTHORS   Yamaguchi,T., Hayashi,T., Takami,H., Nakasone,K., Ohnishi,M.,
            Nakayama,K., Yamada,S., Komatsuzawa,H. and Sugai,M.
  TITLE     Phage conversion of exfoliative toxin A production in
            Staphylococcus aureus
  JOURNAL   Mol Microbiol 38 (4), 694-705 (2000)
   PUBMED   11115106
REFERENCE   2  (residues 1 to 470)
  CONSRTM   NCBI Genome Project
  TITLE     Direct Submission
  JOURNAL   Submitted (09-DEC-2022) National Center for Biotechnology
            Information, NIH, Bethesda, MD 20894, USA
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Sugai,M., Yamaguchi,T., Hayashi,T., Nakasone,K. and Takami,H.
  TITLE     Direct Submission
  JOURNAL   Submitted (28-MAR-2000) Contact:Motoyuki Sugai Hiroshima University
            Faculty of Dentistry, Microbiology; Kasumi 1-2-3, Hiroshima,
            Hiroshima 734-8553, Japan
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence is identical to BAA97651.
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Staphylococcus phage phiETA"
                     /host="Staphylococcus aureus E-1"
                     /db_xref="taxon:2993860"
                     /note="synonym: Bacteriophage phi ETA"
     Protein         1..470
                     /product="endolysin"
                     /calculated_mol_wt=53103
     Region          31..113
                     /region_name="CHAP"
                     /note="CHAP domain; pfam05257"
                     /db_xref="CDD:461605"
     Region          171..357
                     /region_name="MurNAc-LAA"
                     /note="N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA
                     (also known as peptidoglycan aminohydrolase, NAMLA
                     amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC
                     3.5.1.28) is an autolysin that hydrolyzes the amide bond
                     between N-acetylmuramoyl and L-amino...; cl02713"
                     /db_xref="CDD:470658"
     Site            order(177,195,264,329)
                     /site_type="active"
                     /db_xref="CDD:119407"
     Site            order(177,195,264)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:119407"
     CDS             1..470
                     /locus_tag="phiETA_65"
                     /coded_by="NC_003288.1:40341..41753"
                     /note="ORF65;
                     similar to phage phi PVL amidase"
                     /transl_table=11
                     /db_xref="GeneID:927394"
ORIGIN      
        1 mpsvrtysqa isylkslegk awnpdnafgc qcfdtanqyw lylfnhrlkg vgaadiptwn
       61 dftneatvye ntvsfqalpg dvvifnrnyg ggyghvgivi satldsitil eqnwlggayw
      121 sppevttrrt hgydfpmwfi rpfyaketta nklrsavtpv kqdklskgkk imlvaghgig
      181 aysndpgava ngenerdfnr kniiprvkky lesvgntvll yggnsmnqdl yqdtlygqrv
      241 gnykdygmyw iksevkpdai iefhldsasp qasgghviis drfpaddidk alssaldktv
      301 gkirgvtprg dllnanvsad lnlnyrliel gfitstkdln yiknnldsft kriaeaingr
      361 qidapsskps tdkitwnwkg vfypnpekai rvrktagltg tvveedswly tkddwvkfdq
      421 vikkdgywwi rfkyqregss tndffcavcr itdkeqkikn ekywgtiewn