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
- Functionsserine-type D-Ala-D-Ala carboxypeptidase activityProcessescell wall organization / peptidoglycan biosynthetic process / regulation of cell shape / response to antibioticComponentsextracellular 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
- Peptidase_S13 (PF02113)
- 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
Resource Link UniProtKB ID P39045 UniProtKB Entry Name DAC_ACTSP GenBank Gene ID X64790 PDB ID(s) 1W79, 1W8Q, 1W8Y, 2VGJ, 2VGK, 2WKE, 2XDM, 2XK1, 2XLN, 2Y4A, 2Y55, 2Y59, 3ZCZ, 3ZVT, 3ZVW, 4B4X, 4B4Z, 4BEN - General References
- 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]
- 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]
- 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]
- 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]
- 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
Drug Drug group Pharmacological action? Type Actions Details (2R)-2-{(1R)-2-oxo-1-[(2-thienylacetyl)amino]ethyl}-5,6-dihydro-2h-1,3-thiazine-4-carboxylic acid experimental unknown target Details