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LOCUS WP_010989349 242 aa linear BCT 10-APR-2024 ACCESSION WP_010989349 VERSION WP_010989349.1 KEYWORDS RefSeq. SOURCE Listeria ORGANISM Listeria Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae. REFERENCE 1 (residues 1 to 242) AUTHORS Vollmer,W., Joris,B., Charlier,P. and Foster,S. TITLE Bacterial peptidoglycan (murein) hydrolases JOURNAL FEMS Microbiol Rev 32 (2), 259-286 (2008) PUBMED 18266855 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 :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10119458 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..242 /organism="Listeria" /db_xref="taxon:1637" Protein 1..242 /product="N-acetylmuramoyl-L-alanine amidase" /EC_number="3.5.1.28" /GO_function="GO:0008745 - N-acetylmuramoyl-L-alanine amidase activity [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /calculated_mol_wt=26344 Region 3..172 /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...; cd02696" /db_xref="CDD:119407" Site order(10,24,77,142) /site_type="active" /db_xref="CDD:119407" Site order(10,24,77) /site_type="metal-binding" /note="metal binding site [ion binding]" /db_xref="CDD:119407" ORIGIN 1 mtkiwidagh ggkdsgasgn glveknwvlt vakqlqtelv kagfevgmtr tndtfyelsd 61 rakkansfka dlfislhfna gggkgyedyi ytsvpaatve iqkiihknii tkvtkhgmnd 121 rgmkkanfav lretamdail leagfcdstd alilekkayq tdyclgivsa vqeifgamvt 181 kyragkylts ddaisgtnik gyleagtkvf vyketektln ltttkgvpgs wvlktevntg 241 kr