D-alanyl-D-alanine carboxypeptidase dacB (P24228)

Identification
Name:D-alanyl-D-alanine carboxypeptidase dacB
Synonyms:
  • DD-carboxypeptidase
  • DD-peptidase
  • D-alanyl-D-alanine endopeptidase
  • DD-endopeptidase
  • Penicillin-binding protein 4
  • PBP-4
Gene Name:dacB
Enzyme Class:
Biological Properties
General Function:Involved in serine-type carboxypeptidase activity
Specific Function:Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction
Cellular Location:Periplasm (Potential)
SMPDB Pathways:Not Available
KEGG Pathways:
EcoCyc Reactions:
1.0peptidoglycan D-alanyl-DAP crosslink+1.0Thumb ↔ 1.0peptidoglycan tetrapeptide, glycan chain 2+1.0peptidoglycan tetrapeptide, glycan chain 1
1.0peptidoglycan D-alanyl-DAP crosslink + 1.0Water ↔ 1.0peptidoglycan tetrapeptide, glycan chain 2 + 1.0peptidoglycan tetrapeptide, glycan chain 1
ReactionCard
Complex Reactions:
1.0Thumb+1.0three disacharide linked murein units (pentapeptide crosslinked tetrapeptide (A2pm->D-ala) tetrapeptide corsslinked tetrapeptide (A2pm->D-ala)) (middle of chain) → 1.0Thumb+1.0three disacharide linked murein units (tetrapeptide crosslinked tetrapeptide (A2pm->D-ala) & tetrapeptide corsslinked tetrapeptide (A2pm->D-ala)) (middle of chain)
1.0Water + 1.0three disacharide linked murein units (pentapeptide crosslinked tetrapeptide (A2pm->D-ala) tetrapeptide corsslinked tetrapeptide (A2pm->D-ala)) (middle of chain) → 1.0D-Alanine + 1.0three disacharide linked murein units (tetrapeptide crosslinked tetrapeptide (A2pm->D-ala) & tetrapeptide corsslinked tetrapeptide (A2pm->D-ala)) (middle of chain)
ReactionCard
1.0Thumb+1.0two disacharide linked murein units, pentapeptide crosslinked tetrapeptide (A2pm->D-ala) (middle of chain) → 1.0Thumb+1.0two disacharide linked murein units, tetrapeptide corsslinked tetrapeptide (A2pm->D-ala) (middle of chain)
1.0Water + 1.0two disacharide linked murein units, pentapeptide crosslinked tetrapeptide (A2pm->D-ala) (middle of chain) → 1.0D-Alanine + 1.0two disacharide linked murein units, tetrapeptide corsslinked tetrapeptide (A2pm->D-ala) (middle of chain)
ReactionCard
1.0Thumb+1.0two linked disacharide pentapeptide and tetrapeptide murein units (uncrosslinked, middle of chain) → 1.0Thumb+1.0two linked disacharide tetrapeptide murein units (uncrosslinked, middle of chain)
1.0Water + 1.0two linked disacharide pentapeptide and tetrapeptide murein units (uncrosslinked, middle of chain) → 1.0D-Alanine + 1.0two linked disacharide tetrapeptide murein units (uncrosslinked, middle of chain)
ReactionCard
1.0Thumb+1.0two linked disacharide pentapeptide and tripeptide murein units (uncrosslinked, middle of chain) → 1.0Thumb+1.0two linked disacharide tetrapeptide and tripeptide murein units (uncrosslinked, middle of chain)
1.0Water + 1.0two linked disacharide pentapeptide and tripeptide murein units (uncrosslinked, middle of chain) → 1.0D-Alanine + 1.0two linked disacharide tetrapeptide and tripeptide murein units (uncrosslinked, middle of chain)
ReactionCard
1.0Thumb+1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) → 1.0Thumb+1.0two linked disacharide pentapeptide and tetrapeptide murein units (uncrosslinked, middle of chain)
1.0Water + 1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) → 1.0D-Alanine + 1.0two linked disacharide pentapeptide and tetrapeptide murein units (uncrosslinked, middle of chain)
ReactionCard
1.0Thumb+1.0three disacharide linked murein units (tetrapeptide crosslinked tetrapeptide (A2pm->D-ala) & tetrapeptide corsslinked tetrapeptide (A2pm->D-ala)) (middle of chain) → 1.0three disacharide linked murein units (tetrapeptide crosslinked tetrapeptide (A2pm->D-ala), one uncrosslinked tetrapaptide) (middle of chain)
1.0Water + 1.0three disacharide linked murein units (tetrapeptide crosslinked tetrapeptide (A2pm->D-ala) & tetrapeptide corsslinked tetrapeptide (A2pm->D-ala)) (middle of chain) → 1.0three disacharide linked murein units (tetrapeptide crosslinked tetrapeptide (A2pm->D-ala), one uncrosslinked tetrapaptide) (middle of chain)
ReactionCard
1.0Thumb+1.0two disacharide linked murein units, pentapeptide crosslinked tetrapeptide (A2pm->D-ala) (middle of chain) → 1.0two linked disacharide pentapeptide and tetrapeptide murein units (uncrosslinked, middle of chain)
1.0Water + 1.0two disacharide linked murein units, pentapeptide crosslinked tetrapeptide (A2pm->D-ala) (middle of chain) → 1.0two linked disacharide pentapeptide and tetrapeptide murein units (uncrosslinked, middle of chain)
ReactionCard
1.0Thumb+1.0two disacharide linked murein units, tetrapeptide corsslinked tetrapeptide (A2pm->D-ala) (middle of chain) → 1.0two linked disacharide tetrapeptide murein units (uncrosslinked, middle of chain)
1.0Water + 1.0two disacharide linked murein units, tetrapeptide corsslinked tetrapeptide (A2pm->D-ala) (middle of chain) → 1.0two linked disacharide tetrapeptide murein units (uncrosslinked, middle of chain)
ReactionCard
1.0Thumb+1.0two disacharide linked murein units, tripeptide crosslinked tetrapeptide (A2pm->D-ala) (middle of chain) → 1.0two linked disacharide tetrapeptide and tripeptide murein units (uncrosslinked, middle of chain)
1.0Water + 1.0two disacharide linked murein units, tripeptide crosslinked tetrapeptide (A2pm->D-ala) (middle of chain) → 1.0two linked disacharide tetrapeptide and tripeptide murein units (uncrosslinked, middle of chain)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01310D-AlanineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
carboxypeptidase activity
catalytic activity
exopeptidase activity
hydrolase activity
peptidase activity
peptidase activity, acting on L-amino acid peptides
serine-type carboxypeptidase activity
Process
macromolecule metabolic process
metabolic process
protein metabolic process
proteolysis
Gene Properties
Blattner:b3182
Gene OrientationClockwise
Centisome Percentage:71.71
Left Sequence End3326985
Right Sequence End3328418
Gene Sequence:
>1434 bp
ATGTGGCCGGATAACCGTATCGCCCGTGACGCGCACTATCTTTACCGGTATGACCGTCAC
GGCAGGCTGACGGAGAAAACCGACCTCATCCCGGAAGGGGTTATCCGCACGGATGATGAG
CGCACCCACCGGTACCATTACGACAGTCAGCACCGGCTGGTGCACTACACGCGGACACAA
TATGCAGAGCCGCTGGTCGAAAGCCGCTATCTTTACGACCCGCTGGGCCGCAGGGTGGCA
AAACGGGTGTGGCGACGTGAACGGGACCTGACGGGCTGGATGTCGCTGTCACGGAAACCG
CAAGTGACCTGGTACGGCTGGGACGGCGACCGCCTGACCACGATACAGAACGACAGAACC
CGCATCCAGACGATTTATCAGCCGGGGAGCTTCACGCCACTCATCAGGGTTGAAACCGCC
ACCGGTGAGCTGGCGAAAACGCAGCGCCGCAGCCTGGCGGATACCCTTCAGCAGTCCGGC
GGCGAAGACGGTGGCAGTGTGGTGTTCCCGCCGGTGCTGGTGCAGATGCTCGACCGGCTG
GAAAGTGAAATCCTGGCTGACCGGGTGAGTGAGGAAAGCCGCCGCTGGCTGGCATCGTGC
GGCCTGACGGTGGAGCAGATGCAAAACCAGATGGACCCGGTGTACACGCCGGCGCGAAAA
ATCCACCTGTACCACTGCGACCATCGCGGCCTGCCGCTGGCGCTTGTCAGCACGGAAGGG
GCAACAGAATGGTGCGCAGAATACGATGAATGGGGCAACCTGCTGAATGAAGAGAACCCG
CATCAGCTGCAGCAGCTTATCCGCCTGCCGGGGCAGCAGTATGATGAGGAGTCCGGCCTG
TATTACAACCGCCACCGCTATTATGACCCGCTGCAGGGGAGGTATATCACTCAGGATCCG
ATTGGGCTGAAGGGGGGATGGAATTTTTATCAGTATCCGCTGAATCCGGTTCAGTATATA
GATTCAATGGGACTGGCATCAAAATATGGACACTTAAATAATGGCGGATATGGAGCGAGA
CCCAACAAACCGCCTACGCCCGATCCAAGTAAATTGCCGGACATAGCGAAACAATTAAGA
CTGCCATATCCTATTGACCAGGCCAGTAGTGCGCCTAATGTTTTCAAAACATTCTTCAGA
GCATTAAGCCCTTACGACTACACACTGTATTGCAGGAAGTGGGTAAAACCAAATCTGACT
TGTACGCCACAGGATGATTCCCAGTATCCAGGGATGGATACAAAGACAGCAAGTGATTAC
CTGCCACAGACAAATTGGCCAACAACTCAATTACCACCAGGATATACTTGTGCAGAACCC
TATTTATTCCCAGACATTAATAAACCCGATGGGCCAGCAACAGCAGGGATAGATGATTTG
GGTGAAATTTTAGCTAAGATGAAACAGAGAACATCGAGAGGAATAAGAAAATGA
Protein Properties
Pfam Domain Function:
Protein Residues:477
Protein Molecular Weight:51798
Protein Theoretical pI:9
Signaling Regions:
  • 1-20
Transmembrane Regions:
  • None
Protein Sequence:
>D-alanyl-D-alanine carboxypeptidase dacB
MRFSRFIIGLTSCIAFSVQAANVDEYITQLPAGANLALMVQKVGASAPAIDYHSQQMALP
ASTQKVITALAALIQLGPDFRFTTTLETKGNVENGVLKGDLVARFGADPTLKRQDIRNMV
ATLKKSGVNQIDGNVLIDTSIFASHDKAPGWPWNDMTQCFSAPPAAAIVDRNCFSVSLYS
APKPGDMAFIRVASYYPVTMFSQVRTLPRGSAEAQYCELDVVPGDLNRFTLTGCLPQRSE
PLPLAFAVQDGASYAGAILKDELKQAGITWSGTLLRQTQVNEPGTVVASKQSAPLHDLLK
IMLKKSDNMIADTVFRMIGHARFNVPGTWRAGSDAVRQILRQQAGVDIGNTIIADGSGLS
RHNLIAPATMMQVLQYIAQHDNELNFISMLPLAGYDGSLQYRAGLHQAGVDGKVSAKTGS
LQGVYNLAGFITTASGQRMAFVQYLSGYAVEPADQRNRRIPLVRFESRLYKDIYQNN
References
External Links:
ResourceLink
Uniprot ID:P24228
Uniprot Name:DACB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651310
Ecogene ID:EG10202
Ecocyc:EG10202
ColiBase:b3182
Kegg Gene:b3182
EchoBASE ID:EB0198
CCDB:DACB_ECOLI
BacMap:16131072
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kishida, H., Unzai, S., Roper, D. I., Lloyd, A., Park, S. Y., Tame, J. R. (2006). "Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics." Biochemistry 45:783-792. Pubmed: 16411754
  • Korat, B., Mottl, H., Keck, W. (1991). "Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition." Mol Microbiol 5:675-684. Pubmed: 2046551
  • Mottl, H., Terpstra, P., Keck, W. (1991). "Penicillin-binding protein 4 of Escherichia coli shows a novel type of primary structure among penicillin-interacting proteins." FEMS Microbiol Lett 62:213-220. Pubmed: 2040429