MULTISPECIES: phospho-N-acetylmuramoyl-pentapeptide-transferase

LOCUS       WP_003094129             360 aa            linear   BCT 17-JUN-2024
            [Pseudomonas].
ACCESSION   WP_003094129
VERSION     WP_003094129.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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..360
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..360
                     /gene="mraY"
     Protein         1..360
                     /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=39522
     Region          37..360
                     /region_name="GT_MraY-like"
                     /note="Glycosyltransferase 4 (GT4) includes both
                     eukaryotic and prokaryotic
                     UDP-D-N-acetylhexosamine:polyprenol phosphate
                     D-N-acetylhexosamine-1-phosphate transferases. They
                     catalyze the transfer of a D-N-acetylhexosamine
                     1-phosphate to a membrane-bound...; cl10571"
                     /db_xref="CDD:471988"
     Site            115..116
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133462"
     Site            264..267
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133462"
     Site            order(317,323..327)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:133462"
ORIGIN      
        1 mllllaeylq qfykgfgvfq yltlrgilsv ltalslslwl gpwmirtlqi rqigqavrnd
       61 gpqshlskkg tptmggalil taiaistllw adlsnryvwv vlvvtllfga igwvddyrkv
      121 ieknsrglps rwkyfwqsvf gigaavflym taetpiettl ivpmlksvei qlgiffvvlt
      181 yfvivgssna vnltdgldgl aimptvmvag algifcylsg nvkfaeylli pnvpgageli
      241 vfcaalvgag lgflwfntyp aqvfmgdvga lalgaalgti avivrqeivl fimggvfvme
      301 tlsvmiqvas fkltgrrvfr mapihhhfel kgwpeprviv rfwiitvilv liglatlklr