D-alanyl-D-alanine carboxypeptidase

Details

Name
D-alanyl-D-alanine carboxypeptidase
Kind
protein
Synonyms
  • 3.4.16.4
  • DD-carboxypeptidase
  • PBP
  • Penicillin-binding protein
Gene Name
dac
UniProtKB Entry
P39045Swiss-Prot
Organism
Actinomadura sp. (strain R39)
NCBI Taxonomy ID
72570
Amino acid sequence
>lcl|BSEQ0017072|D-alanyl-D-alanine carboxypeptidase
MKQSSPEPLRPRRTGGRGGARRAAALVTIPLLPMTLLGASPALADASGARLTELREDIDA
ILEDPALEGAVSGVVVVDTATGEELYSRDGGEQLLPASNMKLFTAAAALEVLGADHSFGT
EVAAESAPGRRGEVQDLYLVGRGDPTLSAEDLDAMAAEVAASGVRTVRGDLYADDTWFDS
ERLVDDWWPEDEPYAYSAQISALTVAHGERFDTGVTEVSVTPAAEGEPADVDLGAAEGYA
ELDNRAVTGAAGSANTLVIDRPVGTNTIAVTGSLPADAAPVTALRTVDEPAALAGHLFEE
ALESNGVTVKGDVGLGGVPADWQDAEVLADHTSAELSEILVPFMKFSNNGHAEMLVKSIG
QETAGAGTWDAGLVGVEEALSGLGVDTAGLVLNDGSGLSRGNLVTADTVVDLLGQAGSAP
WAQTWSASLPVAGESDPFVGGTLANRMRGTAAEGVVEAKTGTMSGVSALSGYVPGPEGEL
AFSIVNNGHSGPAPLAVQDAIAVRLAEYAGHQAPEGARMMRGPVQGSGELECSWVQAC
Number of residues
538
Molecular Weight
54973.425
Theoretical pI
3.98
GO Classification
Functions
serine-type D-Ala-D-Ala carboxypeptidase activity
Processes
cell wall organization / peptidoglycan biosynthetic process / regulation of cell shape / response to antibiotic
Components
extracellular region
General Function
Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
Specific Function
serine-type D-Ala-D-Ala carboxypeptidase activity
Pfam Domain Function
Signal Regions
1-49
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0006547|1617 bp
ATGAAGCAATCCTCCCCCGAACCCCTGCGCCCCCGCCGCACCGGAGGGCGCGGCGGCGCC
CGGAGGGCCGCCGCCCTCGTCACGATCCCCCTGCTGCCGATGACGCTCCTGGGAGCGTCC
CCCGCGCTCGCCGACGCCTCCGGAGCCCGCCTGACCGAACTGCGCGAGGACATCGACGCC
ATCCTGGAGGACCCCGCACTGGAGGGCGCCGTGTCGGGGGTGGTCGTCGTGGACACCGCG
ACCGGCGAGGAGCTGTACTCGCGCGACGGCGGCGAGCAGCTGCTGCCCGCCTCCAACATG
AAGCTGTTCACCGCGGCCGCCGCCCTGGAGGTCCTGGGCGCCGACCACTCCTTCGGGACC
GAGGTCGCGGCCGAGTCCGCTCCCGGGCGCCGGGGAGAGGTGCAGGACCTCTACCTGGTG
GGCCGGGGCGACCCGACGCTCTCCGCCGAGGACCTGGACGCCATGGCCGCCGAGGTCGCG
GCCTCCGGGGTCCGCACGGTCAGGGGCGACCTGTACGCCGACGACACGTGGTTCGACTCC
GAGCGGCTCGTGGACGACTGGTGGCCCGAGGACGAGCCCTACGCCTACTCGGCCCAGATC
TCGGCCCTGACGGTCGCCCACGGGGAGCGCTTCGACACCGGCGTGACGGAGGTCTCGGTG
ACCCCCGCGGCGGAGGGCGAGCCCGCCGACGTGGACCTCGGCGCCGCGGAGGGCTACGCC
GAGCTCGACAACCGGGCCGTCACCGGCGCCGCCGGCAGCGCCAACACCCTCGTCATCGAC
CGCCCGGTGGGCACCAACACCATCGCGGTCACCGGCTCGCTCCCCGCGGACGCCGCACCC
GTGACCGCGCTGCGGACGGTCGACGAGCCCGCCGCGCTCGCGGGCCACCTCTTCGAGGAG
GCGCTGGAGAGCAACGGCGTCACGGTGAAGGGCGACGTCGGCCTGGGCGGTGTCCCCGCC
GACTGGCAGGACGCCGAGGTGCTCGCCGACCACACGTCGGCCGAGCTCTCCGAGATCCTC
GTGCCCTTCATGAAGTTCAGCAACAACGGGCACGCCGAGATGCTGGTCAAGAGCATCGGC
CAGGAGACCGCCGGCGCGGGCACCTGGGACGCCGGGCTCGTCGGCGTGGAGGAAGCGCTG
TCCGGCCTGGGCGTGGACACCGCCGGCCTGGTCCTCAACGACGGCTCCGGCCTGTCGCGG
GGCAACCTGGTCACCGCGGACACCGTCGTCGACCTGCTCGGGCAGGCGGGTTCCGCCCCC
TGGGCGCAGACCTGGTCCGCCTCGCTGCCGGTCGCGGGCGAGAGCGACCCGTTCGTCGGC
GGCACCCTCGCCAACCGGATGCGCGGTACCGCCGCCGAGGGCGTGGTCGAGGCCAAGACC
GGGACGATGAGCGGGGTCAGCGCCCTCTCCGGGTACGTGCCCGGGCCGGAGGGCGAGCTG
GCGTTCAGCATCGTGAACAACGGCCACTCCGGTCCCGCGCCCCTCGCGGTGCAGGACGCG
ATCGCGGTGCGCCTGGCCGAGTACGCGGGCCACCAGGCGCCGGAGGGCGCCAGGATGATG
CGCGGCCCGGTCCAGGGCAGCGGCGAGCTGGAGTGCTCCTGGGTGCAGGCCTGCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP39045
UniProtKB Entry NameDAC_ACTSP
GenBank Gene IDX64790
PDB ID(s)1W79, 1W8Q, 1W8Y, 2VGJ, 2VGK, 2WKE, 2XDM, 2XK1, 2XLN, 2Y4A, 2Y55, 2Y59, 3ZCZ, 3ZVT, 3ZVW, 4B4X, 4B4Z, 4BEN
General References
  1. Granier B, Duez C, Lepage S, Englebert S, Dusart J, Dideberg O, Van Beeumen J, Frere JM, Ghuysen JM: Primary and predicted secondary structures of the Actinomadura R39 extracellular DD-peptidase, a penicillin-binding protein (PBP) related to the Escherichia coli PBP4. Biochem J. 1992 Mar 15;282 ( Pt 3):781-8. [Article]
  2. Granier B, Duez C, Lepage S, Englebert S, Dusart J, Dideberg O, Van Beeumen J, Frere JM, Ghuysen JM: Primary and predicted secondary structure of the Actinomadura R39 extracellular DD-peptidase, a penicillin-binding protein (PBP) related to the Escherichia coli PBP4. Biochem J. 1992 Sep 15;286 ( Pt 3):981-2. [Article]
  3. Duez C, Joris B, Frere JM, Ghuysen JM, Van Beeumen J: The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39. Biochem J. 1981 Jan 1;193(1):83-6. [Article]
  4. Duez C, Vanhove M, Gallet X, Bouillenne F, Docquier J, Brans A, Frere J: Purification and characterization of PBP4a, a new low-molecular-weight penicillin-binding protein from Bacillus subtilis. J Bacteriol. 2001 Mar;183(5):1595-9. [Article]
  5. Sauvage E, Herman R, Petrella S, Duez C, Bouillenne F, Frere JM, Charlier P: Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins. J Biol Chem. 2005 Sep 2;280(35):31249-56. Epub 2005 Jun 29. [Article]

Associated Data

Drug Relations
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