| IED ID | IndEnz0002018632 |
| Enzyme Type ID | protease018632 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase DacA DD-carboxypeptidase DD-peptidase EC 3.4.16.4 Penicillin-binding protein 5 PBP-5 |
| Gene Name | dacA HI_0029 |
| Organism | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pasteurellales Pasteurellaceae Haemophilus Haemophilus influenzae Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
| Enzyme Sequence | MLKRTTKIAFLSSFVALSAFSVSAEDMQFGVTPPQITAQTYVLMDYNSGAILTALNPDQRQYPASLTKMMTSYVVGVALKQGKIHNTDMVTIGESAWGRNFPDSSKMFLDLNTQVSVADLNRGVIVVSGNDATVALAEHISGNVPNFVETMNKYVQQFGLKNTNFTTPHGLDDPNQYSSARDMAIIGAHIIRDLPEEYKIYSEKNFTFNKIKQANRNGLLWDKTINVDGMKTGHTSQAGYNLVASATTSNNMRLISVVMGVPTYKGREVESKKLLQWGFANFETFKTLEAGKEISEQRVYYGDKNSVKLGALMDHFITIPKGKQSEVKARYELADKNLQAPLVKGQVIGKVVYQLDGKDIASANLQVMNDVGEAGIFGKLWDWLVLTVKGLFS |
| Enzyme Length | 393 |
| Uniprot Accession Number | P44466 |
| Absorption | |
| Active Site | ACT_SITE 65; /note=Acyl-ester intermediate; /evidence=ECO:0000250; ACT_SITE 68; /note=Proton acceptor; /evidence=ECO:0000250; ACT_SITE 128; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 231; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; |
| DNA Binding | |
| EC Number | 3.4.16.4 |
| Enzyme Function | FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (16); Binding site (1); Chain (1); Helix (11); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Carboxypeptidase;Cell inner membrane;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Hydrolase;Membrane;Peptidoglycan synthesis;Protease;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=N-terminal lies in the periplasmic space. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3A3J; |
| Mapped Pubmed ID | 19958776; |
| Motif | |
| Gene Encoded By | |
| Mass | 43,414 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |