| Accession | TIGR00666 |
| Name | PBP4 |
| Function | D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase |
| Gene Symbol | dacB |
| Trusted Cutoff | 107.80 |
| Domain Trusted Cutoff | 107.80 |
| Noise Cutoff | 75.45 |
| Domain Noise Cutoff | 75.45 |
| Isology Type | equivalog |
| EC Number | 3.4.16.4 |
| HMM Length | 397 |
| Mainrole Category | Cell envelope |
| Subrole Category | Biosynthesis and degradation of murein sacculus and peptidoglycan |
| Gene Ontology Term | GO:0008717: D-alanyl-D-alanine endopeptidase activity molecular_function |
| | GO:0009002: serine-type D-Ala-D-Ala carboxypeptidase activity molecular_function |
| | GO:0009252: peptidoglycan biosynthetic process biological_process |
| Author | Haft DH, Loftus BJ |
| Entry Date | Jan 13 2000 2:40PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | In E. coli, this protein is known as penicillin binding protein 4 (dacB). A signal sequence is cleaved from a precursor form. The protein is described as periplasmic in E. coli (Gram-negative) and extracellular in Actinomadura R39 (Gram-positive). Unlike some other proteins with similar activity, it does not form transpeptidation. It is not essential for viability. This family is related to class A beta-lactamases. |
| References | A2 hmmalign
AL manual
RN [1]
RM 91250093
RN [2]
RM 92207168
RT Primary and predicted secondary structures of the Actinomadura R39 extracellular DD-peptidase, a penicillin-binding protein (PBP) related to the Escherichia coli PBP4.
RA Granier B, Duez C, Lepage S, Englebert S, Dusart J, Dideberg O, Van Beeumen J, Frere JM, Ghuysen JM
RL Biochem J 1992 Mar 15;282 ( Pt 3):781-8
DR ECOCYC; EG10202; dacB |
