Detail Information for IndEnz0002018455
IED ID IndEnz0002018455
Enzyme Type ID protease018455
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 Z0777 ECs0670
Organism Escherichia coli O157:H7
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O157:H7
Enzyme Sequence MNTIFSARIMKRLALTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADFAAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNSSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG
Enzyme Length 403
Uniprot Accession Number P0AEB4
Absorption
Active Site ACT_SITE 73; /note=Acyl-ester intermediate; /evidence=ECO:0000250; ACT_SITE 76; /note=Proton acceptor; /evidence=ECO:0000250; ACT_SITE 139; /evidence=ECO:0000250
Activity Regulation
Binding Site BINDING 242; /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); Binding site (1); Chain (1); Sequence conflict (1); Signal peptide (1)
Keywords 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..29; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 44,444
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda