D-alanyl-D-alanine endopeptidase (P0AFI5)

Identification
Name:D-alanyl-D-alanine endopeptidase
Synonyms:
  • DD-endopeptidase
  • Penicillin-binding protein 7
  • PBP-7
Gene Name:pbpG
Enzyme Class:Not Available
Biological Properties
General Function:Involved in serine-type D-Ala-D-Ala carboxypeptidase activity
Specific Function:Cell wall formation. May play a specialized role in remodeling the cell wall. Specifically hydrolyze the DD- diaminopimelate-alanine bonds in high-molecular-mass murein sacculi
Cellular Location:Periplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
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 (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
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
serine-type D-Ala-D-Ala carboxypeptidase activity
Process
macromolecule metabolic process
metabolic process
protein metabolic process
proteolysis
Gene Properties
Blattner:b2134
Gene OrientationCounterclockwise
Centisome Percentage:47.89
Left Sequence End2221960
Right Sequence End2222892
Gene Sequence:
>933 bp
ATGGTTAAAGTTTATGCCCCGGCTTCCAGTGCCAATATGAGCGTCGGGTTTGATGTGCTC
GGGGCGGCGGTGACACCTGTTGATGGTGCATTGCTCGGAGATGTAGTCACGGTTGAGGCG
GCAGAGACATTCAGTCTCAACAACCTCGGACGCTTTGCCGATAAGCTGCCGTCAGAACCA
CGGGAAAATATCGTTTATCAGTGCTGGGAGCGTTTTTGCCAGGAACTGGGTAAGCAAATT
CCAGTGGCGATGACCCTGGAAAAGAATATGCCGATCGGTTCGGGCTTAGGCTCCAGTGCC
TGTTCGGTGGTCGCGGCGCTGATGGCGATGAATGAACACTGCGGCAAGCCGCTTAATGAC
ACTCGTTTGCTGGCTTTGATGGGCGAGCTGGAAGGCCGTATCTCCGGCAGCATTCATTAC
GACAACGTGGCACCGTGTTTTCTCGGTGGTATGCAGTTGATGATCGAAGAAAACGACATC
ATCAGCCAGCAAGTGCCAGGGTTTGATGAGTGGCTGTGGGTGCTGGCGTATCCGGGGATT
AAAGTCTCGACGGCAGAAGCCAGGGCTATTTTACCGGCGCAGTATCGCCGCCAGGATTGC
ATTGCGCACGGGCGACATCTGGCAGGCTTCATTCACGCCTGCTATTCCCGTCAGCCTGAG
CTTGCCGCGAAGCTGATGAAAGATGTTATCGCTGAACCCTACCGTGAACGGTTACTGCCA
GGCTTCCGGCAGGCGCGGCAGGCGGTCGCGGAAATCGGCGCGGTAGCGAGCGGTATCTCC
GGCTCCGGCCCGACCTTGTTCGCTCTGTGTGACAAGCCGGAAACCGCCCAGCGCGTTGCC
GACTGGTTGGGTAAGAACTACCTGCAAAATCAGGAAGGTTTTGTTCATATTTGCCGGCTG
GATACGGCGGGCGCACGAGTACTGGAAAACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:310
Protein Molecular Weight:33887
Protein Theoretical pI:11
Signaling Regions:
  • 1-25
Transmembrane Regions:
  • None
Protein Sequence:
>D-alanyl-D-alanine endopeptidase
MPKFRVSLFSLALMLAVPFAPQAVAKTAAATTASQPEIASGSAMIVDLNTNKVIYSNHPD
LVRPIASISKLMTAMVVLDARLPLDEKLKVDISQTPEMKGVYSRVRLNSEISRKDMLLLA
LMSSENRAAASLAHHYPGGYKAFIKAMNAKAKSLGMNNTRFVEPTGLSVHNVSTARDLTK
LLIASKQYPLIGQLSTTREDMATFSNPTYTLPFRNTNHLVYRDNWNIQLTKTGFTNAAGH
CLVMRTVINNKPVALVVMDAFGKYTHFADASRLRTWIETGKVMPVPAAALSYKKQKAAQM
AAAGQTAQND
References
External Links:
ResourceLink
Uniprot ID:P0AFI5
Uniprot Name:PBP7_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674277
Ecogene ID:EG12015
Ecocyc:EG12015
ColiBase:b2134
Kegg Gene:b2134
EchoBASE ID:EB1952
CCDB:PBP7_ECOLI
BacMap:162135905
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
  • Campbell, H. D., Rogers, B. L., Young, I. G. (1984). "Nucleotide sequence of the respiratory D-lactate dehydrogenase gene of Escherichia coli." Eur J Biochem 144:367-373. Pubmed: 6386470
  • 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
  • Henderson, T. A., Templin, M., Young, K. D. (1995). "Identification and cloning of the gene encoding penicillin-binding protein 7 of Escherichia coli." J Bacteriol 177:2074-2079. Pubmed: 7721700
  • Romeis, T., Holtje, J. V. (1994). "Penicillin-binding protein 7/8 of Escherichia coli is a DD-endopeptidase." Eur J Biochem 224:597-604. Pubmed: 7925376