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Literature summary for 3.4.22.70 extracted from

  • Ilangovan, U.; Ton-That, H.; Iwahara, J.; Schneewind, O.; Clubb, R.T.
    Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus (2001), Proc. Natl. Acad. Sci. USA, 98, 6056-6061.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.70

Protein Variants

Protein Variants Comment Organism
DELTA N59 trucation of N-terminal 59 amino acids does not affect the activity of the enzyme Staphylococcus aureus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane class A sortases adopt a type II membrane topology (N terminus inside and C terminus outside the cytoplasm), class B enzymes represent type I membrane proteins (N terminus outside, C terminus inside) Staphylococcus aureus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 2 mM, 8fold stimulation of activity, binding near the active site stimulates catalysis possibly by altering the conformation of a surface loop that recognizes newly translocated polypeptides Staphylococcus aureus
Mg2+ can substitute in part for Ca2+ Staphylococcus aureus
Mn2+ can substitute in part for Ca2+ Staphylococcus aureus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 signal peptide, membrane anchor and a shorter linker domain of sortase enzymes display no amino acid conservation. The core residue, SrtA residues 60-206, is present in all sortase homologs examined, suggesting that this domain may comprise the catalytically active domain Staphylococcus aureus
16595
-
 x * 16595, SrtDELTAN59, electrospray ionization mass spectrometry Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Staphylococcus aureus the enzyme cleaves surface proteins at the LPXTG motif and catalyzes the formation of an amide bond between the carboxyl group of Thr and the amino group of cell-wall crossbridges ?
-
 ?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
 SrtADELTAN, a soluble enzyme lacking the N-terminal signal peptide, residues 2-29 of SrtA and SrtDELTAN59, which contains only the presumed catalytic core
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Leu-Pro-Glu-Thr-Gly-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
-
 Staphylococcus aureus 4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Leu-Pro-Glu-Thr + Gly-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
-
 ?
additional information the enzyme cleaves surface proteins at the LPXTG motif and catalyzes the formation of an amide bond between the carboxyl group of Thr and the amino group of cell-wall crossbridges Staphylococcus aureus ?
-
 ?

Subunits

Subunits Comment Organism
? x * 16595, SrtDELTAN59, electrospray ionization mass spectrometry Staphylococcus aureus