Detail Information for IndEnz0002001762
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