D-alanyl-D-alanine carboxypeptidase

NameD-alanyl-D-alanine carboxypeptidase
Synonyms
  • 3.4.16.4
  • DD-carboxypeptidase
Gene NameNone
OrganismStreptomyces sp. (strain R61)
Amino acid sequence
>lcl|BSEQ0010942|D-alanyl-D-alanine carboxypeptidase
MVSGTVGRGTALGAVLLALLAVPAQAGTAAAADLPAPDDTGLQAVLHTALSQGAPGAMVR
VDDNGTIHQLSEGVADRATGRAITTTDRFRVGSVTKSFSAVVLLQLVDEGKLDLDASVNT
YLPGLLPDDRITVRQVMSHRSGLYDYTNDMFAQTVPGFESVRNKVFSYQDLITLSLKHGV
TNAPGAAYSYSNTNFVVAGMLIEKLTGHSVATEYQNRIFTPLNLTDTFYVHPDTVIPGTH
ANGYLTPDEAGGALVDSTEQTVSWAQSAGAVISSTQDLDTFFSALMSGQLMSAAQLAQMQ
QWTTVNSTQGYGLGLRRRDLSCGISVYGHTGTVQGYYTYAFASKDGKRSVTALANTSNNV
NVLNTMARTLESAFCGKPTTAKLRSATSSATTVERHEDIAPGIARD
Number of residuesNone
Molecular Weight42916.725
Theoretical pI6.03
GO Classification
Functions
  • serine-type D-Ala-D-Ala carboxypeptidase activity
Processes
  • regulation of cell shape
  • cell wall organization
  • peptidoglycan biosynthetic process
Components
  • extracellular region
General FunctionSerine-type d-ala-d-ala carboxypeptidase activity
Specific FunctionCatalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e. a D-alanyl-D-alanine-terminated peptide), it becomes immobilized in the form of a long-lived, serine-ester-linked acyl enzyme and thus behave as penicillin-binding protein (PBP).
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP15555
UniProtKB Entry Name
Cellular LocationSecreted
Gene sequence
>lcl|BSEQ0002678|1221 bp
ATGGTCTCAGGAACGGTGGGCAGAGGTACGGCGCTGGGCGCGGTGCTGTTGGCCCTCCTC
GCAGTCCCCGCACAGGCCGGCACCGCCGCGGCCGCGGATCTGCCGGCACCCGACGACACC
GGTCTGCAGGCGGTGCTGCACACGGCCCTTTCCCAGGGAGCCCCCGGTGCGATGGTGCGG
GTCGACGACAACGGCACGATCCACCAGTTGTCGGAGGGAGTCGCCGACCGGGCCACCGGG
CGTGCGATCACCACGACCGACCGGTTCCGCGTCGGCAGCGTCACCAAGAGCTTCTCCGCC
GTGGTCCTGCTGCAACTGGTGGACGAGGGCAAGCTCGACCTGGACGCTTCGGTGAACACC
TATCTGCCCGGGCTGCTGCCCGACGACCGGATCACCGTGCGTCAGGTGATGAGCCACCGC
AGTGGGCTGTACGACTACACCAACGACATGTTCGCGCAGACGGTCCCGGGCTTCGAGTCC
GTCCGCAACAAGGTCTTCAGCTACCAGGACCTGATCACCCTGTCCCTCAAGCACGGGGTC
ACCAACGCACCGGGCGCGGCCTATTCATACTCCAACACGAACTTCGTCGTCGCGGGCATG
CTCATCGAGAAGCTCACCGGCCACTCCGTGGCCACGGAGTACCAGAACCGCATCTTCACG
CCGCTGAACCTGACCGACACCTTCTACGTGCACCCCGACACCGTCATCCCGGGCACCCAC
GCCAACGGCTACCTCACGCCGGACGAGGCCGGTGGGGCCCTGGTCGACTCCACCGAGCAG
ACGGTGTCGTGGGCGCAGAGCGCGGGCGCGGTCATCTCCAGCACGCAGGACCTGGACACG
TTCTTCTCCGCGTTGATGAGCGGGCAGCTCATGTCCGCCGCGCAGCTCGCGCAGATGCAG
CAGTGGACGACGGTCAACAGCACCCAGGGGTACGGCCTCGGCCTGCGCCGCCGTGACCTG
TCCTGCGGTATCTCGGTGTACGGCCACACGGGCACCGTGCAGGGCTACTACACGTACGCC
TTCGCCTCGAAGGACGGCAAGCGCAGCGTCACCGCGCTCGCCAACACCTCGAACAACGTG
AACGTGCTGAACACGATGGCCCGCACGCTGGAATCCGCGTTCTGCGGCAAGCCGACGACC
GCGAAGCTGCGCAGCGCGACCTCCTCGGCGACCACCGTGGAGCGCCACGAGGACATCGCG
CCGGGTATCGCCCGCGACTGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Duez C, Piron-Fraipont C, Joris B, Dusart J, Urdea MS, Martial JA, Frere JM, Ghuysen JM: Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene. Eur J Biochem. 1987 Feb 2;162(3):509-18. [3830154 ]
  2. Duez C, Piron-Fraipont C, Joris B, Dusart J, Urdea MS, Martial JA, Frere JM, Ghuysen JM: Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene. Eur J Biochem. 1994 Sep 15;224(3):1079. [7925404 ]
  3. Joris B, Jacques P, Frere JM, Ghuysen JM, Van Beeumen J: Primary structure of the Streptomyces R61 extracellular DD-peptidase. 2. Amino acid sequence data. Eur J Biochem. 1987 Feb 2;162(3):519-24. [3030739 ]
  4. Piron-Fraipont C, Lenzini MV, Dusart J, Ghuysen JM: Transcriptional analysis of the DD-peptidase/penicillin-binding protein-encoding dac gene of Streptomyces R61: use of the promoter and signal sequences in a secretion vector. Mol Gen Genet. 1990 Aug;223(1):114-20. [2175384 ]
  5. Knox JR, Pratt RF: Different modes of vancomycin and D-alanyl-D-alanine peptidase binding to cell wall peptide and a possible role for the vancomycin resistance protein. Antimicrob Agents Chemother. 1990 Jul;34(7):1342-7. [2386365 ]
  6. Kelly JA, Knox JR, Moews PC, Hite GJ, Bartolone JB, Zhao H, Joris B, Frere JM, Ghuysen JM: 2.8-A Structure of penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 and complexes with beta-lactams. J Biol Chem. 1985 May 25;260(10):6449-58. [3997832 ]
  7. Kelly JA, Kuzin AP: The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 A resolution. J Mol Biol. 1995 Nov 24;254(2):223-36. [7490745 ]
  8. McDonough MA, Anderson JW, Silvaggi NR, Pratt RF, Knox JR, Kelly JA: Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins. J Mol Biol. 2002 Sep 6;322(1):111-22. [12215418 ]
  9. Silvaggi NR, Anderson JW, Brinsmade SR, Pratt RF, Kelly JA: The crystal structure of phosphonate-inhibited D-Ala-D-Ala peptidase reveals an analogue of a tetrahedral transition state. Biochemistry. 2003 Feb 11;42(5):1199-208. [12564922 ]
  10. Silvaggi NR, Josephine HR, Kuzin AP, Nagarajan R, Pratt RF, Kelly JA: Crystal structures of complexes between the R61 DD-peptidase and peptidoglycan-mimetic beta-lactams: a non-covalent complex with a "perfect penicillin". J Mol Biol. 2005 Jan 21;345(3):521-33. [15581896 ]

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