phospho-N-acetylmuramoyl-pentapeptide-transferase [Listeria

LOCUS       WP_003731978             324 aa            linear   BCT 17-JUN-2024
            monocytogenes].
ACCESSION   WP_003731978
VERSION     WP_003731978.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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  :: HMM
            Evidence Accession :: TIGR00445.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     gene            1..324
                     /gene="mraY"
     Protein         1..324
                     /product="phospho-N-acetylmuramoyl-pentapeptide-
                     transferase"
                     /EC_number="2.7.8.13"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008963 -
                     phospho-N-acetylmuramoyl-pentapeptide-transferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=35637
     Region          41..319
                     /region_name="GT_MraY"
                     /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase
                     (mraY) is an enzyme responsible for the formation of the
                     first lipid intermediate in the synthesis of bacterial
                     cell wall peptidoglycan. It catalyzes the formation of...;
                     cd06852"
                     /db_xref="CDD:133462"
     Site            98..99
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133462"
     Site            228..231
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133462"
     Site            order(282,288..292)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:133462"
ORIGIN      
        1 mslymlvstf avafiitvig vplfipflvk lkfgqsirde gpkmhekksg tptmgavvfi
       61 tamlisflvf sfisgevsaa twllfialal fgalgflddy ikvvqkrnlg ltskqkflgq
      121 vvisilfylv yhfndfaetl nipftnievd lgwffvifil fwlvgfsnav nltdgldglv
      181 sglsviafsa fgviafyqeq mdvaifcfai vggmlgfllf nknpakifmg dtgslalggs
      241 iaaisilvhq ewlllligii fvietasvil qvfyfkatgg krifrmtpih hhfelggwse
      301 wrvvltfwgi glvgaiisvc vvif