Title : 
Sequence analysis of putative N-acetylglucosaminidase, SACOL2666 gene in S. aureus
         
        
            Author : 
Kusnan, Khalida Ain ; Mohamad, Sharifah Aminah Syed ; Latiffi, Amaliawati Ahmad ; Abdullah, Mohd Faiz Foong ; Yunus, Norfatimah Mohamed ; Kamarun, Dzaraini
         
        
            Author_Institution : 
Fac. of Appl. Sci., Univ. Teknol. MARA, Shah Alam, Malaysia
         
        
        
        
        
        
            Abstract : 
A novel N-acetylglucosaminidase encoded by SACOL2666 has been isolated from S. aureus SH1000. The nucleotide sequence of the clone designated pQE60-xSCaQ was determined. The gene is 1860 bp in length and contains an open reading frame from 82 to 1860 bp encoding 592 amino acids residues of mature protein with a predicted molecular weight of 66 kD. BLAST analysis of SACOL2666 nucleotide sequence shows 100% identity with muramoyl-L-alanine amidase from S. aureus COL complete genome and 99% identity with N-acetylglucosaminidase protein family from S. aureus ECT-R2. While the deduced amino acids sequence of SACOL2666 shows 99% homology with N-acetylglucosaminidase family protein S. aureus CIG547 at locus name SACIG547_0476 in NCBI database. Multiple alignments show that SACOL2666 has conserved sequence pattern with characterized N-acetylglucosaminidase (overlapping with amidase domain) than bifunctional domain enzymes (in tandem) such as Atl from S. aureus. SACOL2666 has consensus amino acids at carboxylic active sites reported in Auto, a member of Glycoside hydrolase family. Catalytic sites for N-glucosaminidase D and E were found in SACOL2666 at E352, E386 and D452. Phylogenetic analysis of amino acid sequence from the selected N-acetylglucosaminidase indicated close phylogenetic relationship of SACOL2666 with AcmB than Atl.
         
        
            Keywords : 
enzymes; genetics; molecular biophysics; BLAST analysis; Glycoside hydrolase family; NCBI database; S. aureus; SACIG547_0476; SACOL2666 gene; amino acids; bifunctional domain enzymes; carboxylic active sites; genome; mature protein; molecular weight; muramoyl-L-alanine amidase; nucleotide sequence analysis; pQE60-xSCaQ clone; putative N-acetylglucosaminidase; Amino acids; Bioinformatics; Cloning; Genomics; Proteins; Strain; COL genome; N-acetylglucosaminidase; S. aureus; autolysin; cloning;
         
        
        
        
            Conference_Titel : 
Humanities, Science and Engineering Research (SHUSER), 2012 IEEE Symposium on
         
        
            Conference_Location : 
Kuala Lumpur
         
        
            Print_ISBN : 
978-1-4673-1311-7
         
        
        
            DOI : 
10.1109/SHUSER.2012.6268891