D-alanyl-D-alanine carboxypeptidase

Details

Name
D-alanyl-D-alanine carboxypeptidase
Synonyms
  • 3.4.16.4
  • DD-carboxypeptidase
  • PBP
  • Penicillin-binding protein
Gene Name
dac
Organism
Actinomadura sp. (strain R39)
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
Serine-type d-ala-d-ala carboxypeptidase activity
Specific Function
Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
Pfam Domain Function
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
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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04742(2R)-2-{(1R)-2-oxo-1-[(2-thienylacetyl)amino]ethyl}-5,6-dihydro-2h-1,3-thiazine-4-carboxylic acidexperimentalunknownDetails