Detail Information for IndEnz0002008823
IED ID IndEnz0002008823
Enzyme Type ID protease008823
Protein Name Sortase A
EC 3.4.22.-
Gene Name srtA BAS0654
Organism Bacillus anthracis
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus cereus group Bacillus anthracis
Enzyme Sequence MNKQRIYSIVAILLFVVGGVLIGKPFYDGYQAEKKQTENVQAVQKMDYEKHETEFVDASKIDQPDLAEVANASLDKKQVIGRISIPSVSLELPVLKSSTEKNLLSGAATVKENQVMGKGNYALAGHNMSKKGVLFSDIASLKKGDKIYLYDNENEYEYAVTGVSEVTPDKWEVVEDHGKDEITLITCVSVKDNSKRYVVAGDLVGTKAKK
Enzyme Length 210
Uniprot Accession Number P0DPQ5
Absorption
Active Site ACT_SITE 126; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q2FV99; ACT_SITE 187; /note=Acyl-thioester intermediate; /evidence=ECO:0000250|UniProtKB:Q2FV99
Activity Regulation ACTIVITY REGULATION: Inhibited by thiol-reactive reagents. {ECO:0000269|PubMed:15968076}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.22.-
Enzyme Function FUNCTION: Transpeptidase that anchors surface proteins to the cell wall (PubMed:15968076). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (PubMed:15968076). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:15968076). Important for growth in macrophages. May be critical in the early stages of inhalation anthrax (PubMed:16041044). {ECO:0000269|PubMed:15968076, ECO:0000269|PubMed:16041044}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Mutagenesis (3); Site (1); Topological domain (2); Transmembrane (1)
Keywords 3D-structure;Cell membrane;Hydrolase;Membrane;Protease;Thiol protease;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2FV99}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q2FV99}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D NMR spectroscopy (2)
Cross Reference PDB 2KW8; 2RUI;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 23,151
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda