MULTISPECIES: D-alanyl-D-alanine

LOCUS       WP_003091272             476 aa            linear   BCT 20-NOV-2023
            carboxypeptidase/D-alanyl-D-alanine-endopeptidase [Pseudomonas].
ACCESSION   WP_003091272
VERSION     WP_003091272.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Granier,B., Duez,C., Lepage,S., Englebert,S., Dusart,J.,
            Dideberg,O., Van Beeumen,J., Frere,J.M. and Ghuysen,J.M.
  TITLE     Primary and predicted secondary structures of the Actinomadura R39
            extracellular DD-peptidase, a penicillin-binding protein (PBP)
            related to the Escherichia coli PBP4
  JOURNAL   Biochem. J. 282 (Pt 3), 781-788 (1992)
   PUBMED   1554361
  REMARK    Erratum:[Biochem J. 1992 Sep 15;286 ( Pt 3):981-2. PMID: 1417760]
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Mottl,H., Terpstra,P. and Keck,W.
  TITLE     Penicillin-binding protein 4 of Escherichia coli shows a novel type
            of primary structure among penicillin-interacting proteins
  JOURNAL   FEMS Microbiol. Lett. 62 (2-3), 213-220 (1991)
   PUBMED   2040429
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 :: TIGR00666.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..476
                     /gene="dacB"
     Protein         1..476
                     /product="D-alanyl-D-alanine
                     carboxypeptidase/D-alanyl-D-alanine-endopeptidase"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0004175 - endopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=51730
     Region          13..476
                     /region_name="DacB"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG2027"
                     /db_xref="CDD:441630"
ORIGIN      
        1 mfkslrtlaf atllpfalpt laqvnatlpa nvqkalqtnk ltgndlslvl ipldgpgnpt
       61 yynadvsvnp astmklftty aalemlgpty qwktefytdg qlkngvlngn lylkgggdpk
      121 lnmeklwllm rdlrangvtk vtgdlvldrs yfnipqlpvf nddggddtkp flvgpdsllv
      181 nlksvrmvvr tdgnkvnvqm dpplanvrid nqvkmtapat cpawpklrfs pvtqfdgttl
      241 latgqipqgc saqtymslld hpgytagavr giwqelggsi lgkdrqgsvp rnatliakaf
      301 spdlveiird inkysnntma rqlflsigaq frnsadgdda qaaqrvvrqw larkgitapr
      361 lvmengsgls rqervsarem aamlqaawhs pyaaeyissl plagldgtmr krlrrtalvg
      421 eahvktgtln tvralagfsr dasghnwvvv ailnsprpwg asaildqvll slhark