D-alanyl-D-alanine carboxypeptidase DacB
Details
- Name
- D-alanyl-D-alanine carboxypeptidase DacB
- Synonyms
- 3.4.16.4
- D-alanyl-D-alanine endopeptidase
- DD-carboxypeptidase
- DD-endopeptidase
- PBP-4
- Penicillin-binding protein 4
- Gene Name
- dacB
- UniProtKB Entry
- P24228Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0019003|D-alanyl-D-alanine carboxypeptidase DacB MRFSRFIIGLTSCIAFSVQAANVDEYITQLPAGANLALMVQKVGASAPAIDYHSQQMALP ASTQKVITALAALIQLGPDFRFTTTLETKGNVENGVLKGDLVARFGADPTLKRQDIRNMV ATLKKSGVNQIDGNVLIDTSIFASHDKAPGWPWNDMTQCFSAPPAAAIVDRNCFSVSLYS APKPGDMAFIRVASYYPVTMFSQVRTLPRGSAEAQYCELDVVPGDLNRFTLTGCLPQRSE PLPLAFAVQDGASYAGAILKDELKQAGITWSGTLLRQTQVNEPGTVVASKQSAPLHDLLK IMLKKSDNMIADTVFRMIGHARFNVPGTWRAGSDAVRQILRQQAGVDIGNTIIADGSGLS RHNLIAPATMMQVLQYIAQHDNELNFISMLPLAGYDGSLQYRAGLHQAGVDGKVSAKTGS LQGVYNLAGFITTASGQRMAFVQYLSGYAVEPADQRNRRIPLVRFESRLYKDIYQNN
- Number of residues
- 477
- Molecular Weight
- 51797.85
- Theoretical pI
- 9.02
- GO Classification
- Functionscarboxypeptidase activity / endopeptidase activity / penicillin binding / serine-type D-Ala-D-Ala carboxypeptidase activityProcessescell wall macromolecule catabolic process / cell wall organization / FtsZ-dependent cytokinesis / peptidoglycan biosynthetic process / peptidoglycan catabolic process / peptidoglycan metabolic process / peptidoglycan turnover / regulation of cell shape / response to antibioticComponentsouter membrane-bounded periplasmic space
- General Function
- Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction.
- Specific Function
- carboxypeptidase activity
- Pfam Domain Function
- Peptidase_S13 (PF02113)
- Signal Regions
- 1-20
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0019004|D-alanyl-D-alanine carboxypeptidase DacB (dacB) ATGCGATTTTCCAGATTTATCATCGGATTGACCAGCTGTATAGCGTTCAGTGTTCAGGCC GCAAATGTTGATGAGTACATTACTCAACTCCCCGCTGGTGCCAACCTTGCCCTGATGGTG CAAAAAGTCGGCGCGTCGGCCCCCGCTATTGATTACCACAGTCAGCAGATGGCGCTGCCT GCCAGTACCCAGAAAGTGATTACTGCGCTGGCGGCGTTGATTCAACTCGGCCCCGATTTT CGTTTTACCACGACGCTTGAAACCAAAGGCAATGTGGAAAACGGCGTACTTAAGGGTGAC TTAGTGGCGCGATTTGGTGCCGATCCGACGTTAAAACGTCAGGATATTCGCAATATGGTC GCGACTTTGAAAAAATCTGGCGTCAACCAAATCGATGGCAATGTGTTGATAGATACCTCC ATTTTCGCCAGCCACGATAAAGCCCCCGGCTGGCCATGGAATGACATGACACAATGCTTT AGCGCTCCGCCTGCCGCCGCCATAGTTGACCGCAACTGTTTCTCCGTCTCGCTCTACAGT GCCCCAAAGCCTGGTGATATGGCTTTTATACGCGTGGCATCTTATTACCCCGTTACGATG TTCAGCCAGGTACGCACCCTCCCCCGTGGTTCTGCCGAAGCGCAATACTGCGAACTGGAT GTGGTGCCAGGCGACCTGAACCGCTTTACGCTGACGGGATGCCTGCCACAACGTTCTGAG CCGCTCCCGTTGGCTTTTGCCGTGCAGGATGGAGCCAGCTATGCCGGTGCAATTCTGAAA GATGAGTTAAAACAGGCGGGTATCACCTGGAGCGGAACACTGCTGCGCCAGACTCAGGTT AACGAACCTGGAACGGTAGTTGCCAGTAAACAGTCGGCCCCGCTGCACGATCTGCTTAAG ATTATGCTGAAAAAGTCGGACAACATGATCGCCGATACGGTTTTCCGCATGATAGGCCAT GCGCGCTTCAATGTGCCTGGAACATGGCGGGCCGGGTCGGACGCCGTGCGTCAGATCCTG CGCCAGCAAGCCGGTGTCGATATTGGAAACACCATTATTGCCGATGGTTCAGGGCTTTCG CGGCATAACCTGATTGCCCCCGCCACCATGATGCAGGTGCTGCAATACATTGCCCAACAC GACAATGAACTTAACTTTATCTCCATGCTGCCGCTGGCGGGCTATGACGGCTCTTTGCAG TACCGTGCAGGTCTGCATCAGGCGGGCGTGGATGGAAAAGTCTCAGCGAAAACCGGTTCG TTGCAGGGGGTATATAACCTGGCGGGATTCATTACCACAGCGAGCGGGCAACGAATGGCG TTTGTGCAATATCTTTCTGGCTATGCAGTAGAACCTGCGGATCAGCGTAATCGCCGTATT CCGTTAGTGCGTTTTGAAAGCCGTTTGTATAAAGATATTTATCAGAACAATTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P24228 UniProtKB Entry Name DACB_ECOLI GenBank Protein ID 41216 GenBank Gene ID X59460 PDB ID(s) 2EX2, 2EX6, 2EX8, 2EX9, 2EXA, 2EXB KEGG ID ecj:JW3149 NCBI Gene ID 947693 - General References
- Mottl H, Terpstra P, Keck W: Penicillin-binding protein 4 of Escherichia coli shows a novel type of primary structure among penicillin-interacting proteins. FEMS Microbiol Lett. 1991 Mar 1;62(2-3):213-20. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR: Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics. Biochemistry. 2006 Jan 24;45(3):783-92. [Article]
- Korat B, Mottl H, Keck W: Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition. Mol Microbiol. 1991 Mar;5(3):675-84. [Article]
Associated Data
- Bio-Entities
Bio-Entity Type D-alanyl-D-alanine carboxypeptidase DacB (Escherichia coli (strain K12)) protein primaryPenicillin-binding protein (Gram positive and gram negative bacteria) protein - Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Meropenem approved, investigational yes target inhibitor Details Cefoperazone approved, investigational yes target inhibitor Details Cefoxitin approved yes target inhibitor Details Cefonicid approved, investigational yes target inhibitor Details Ertapenem approved, investigational yes target inhibitor Details Latamoxef approved, investigational unknown target inhibitor Details Phenoxymethylpenicillin approved, vet_approved unknown target Details Cefiderocol approved, investigational yes target inhibitor Details Carbenicillin approved, investigational yes target inhibitor Details Carindacillin approved, investigational yes target inhibitor Details Ceftolozane approved, investigational unknown target Details Bacampicillin approved, investigational yes target inhibitor Details Cyclacillin approved yes target inhibitor Details Cefixime approved, investigational yes target binder Details