IED ID | IndEnz0002001762 |
Enzyme Type ID | protease001762 |
Protein Name |
Sortase A EC 3.4.22.- |
Gene Name | srtA lmo0929 |
Organism | Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Listeriaceae Listeria Listeria monocytogenes Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) |
Enzyme Sequence | MLKKTIAIIILIIGLLLIFSPFIKNGIVKYMSGHETIEQYKASDIKKNNEKDATFDFESVQLPSMTSVIKGAANYDKDAVVGSIAVPSVDVNLLVFKGTNTANLLAGATTMRSDQVMGKGNYPLAGHHMRDESMLFGPIMKVKKGDKIYLTDLENLYEYTVTETKTIDETEVSVIDNTKDARITLITCDKPTETTKRFVAVGELEKTEKLTKELENKYFPSK |
Enzyme Length | 222 |
Uniprot Accession Number | Q8Y8H5 |
Absorption | |
Active Site | ACT_SITE 127; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q2FV99; ACT_SITE 188; /note=Acyl-thioester intermediate; /evidence=ECO:0000250|UniProtKB:Q2FV99 |
Activity Regulation | ACTIVITY REGULATION: Activity is enhanced by Zn(2+) and strongly enhanced by Ca(2+). Inhibited by chalcone, a precursor of several flavonoids, which blocks the SrtA active site. {ECO:0000269|PubMed:26826492}. |
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:11854224, PubMed:11929538, PubMed:16247833, PubMed:22837151). 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 (Probable). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:11929538). Involved in pathogenesis (PubMed:11854224, PubMed:11929538, PubMed:15028680). May regulate the rate of synthesis and/or the stability of a subset of LPXTG proteins (PubMed:22837151). Not involved in cell wall-anchoring of Hbp2 (SvpA) or Hbp1 (PubMed:15028680, PubMed:16247833). {ECO:0000269|PubMed:11854224, ECO:0000269|PubMed:11929538, ECO:0000269|PubMed:15028680, ECO:0000269|PubMed:16247833, ECO:0000269|PubMed:22837151, ECO:0000305|PubMed:11929538}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (9); Chain (1); Helix (4); Mutagenesis (3); Site (1); Topological domain (2); Transmembrane (1); Turn (1) |
Keywords | 3D-structure;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;Thiol protease;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11929538}; Single-pass type II membrane protein {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 5HU4; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 24,712 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |