Sequence of SRTA_STAA8
EC Number:3.4.22.70
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
The enzyme catalyses a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXTG motif is cleaved between the Thr and Gly residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan.
Other sequences found for EC No. 3.4.22.70
General information:
Sequence
0 MKKWTNRLMT IAGVVLILVA AYLFAKPHID NYLHDKDKDE KIEQYDKNVK EQASKDKKQQ
60 AKPQIPKDKS KVAGYIEIPD ADIKEPVYPG PATPEQLNRG VSFAEENESL DDQNISIAGH
120 TFIDRPNYQF TNLKAAKKGS MVYFKVGNET RKYKMTSIRD VKPTDVGVLD EQKGKDKQLT
180 LITCDDYNEK TGVWEKRKIF VATEVK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
102799
Mazmanian S.K.,Liu G.,Ton-That H.,Schneewind O.
Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall.
Science
285
760-763
1999
102800
Ton-That H.,Schneewind O.
Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the cell wall sorting reaction.
J. Biol. Chem.
274
24316-24320
1999
102801
Ton-That H.,Liu G.,Mazmanian S.K.,Faull K.F.,Schneewind O.
Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif.
Proc. Natl. Acad. Sci. U.S.A.
96
12424-12429
1999
102802
Mazmanian S.K.,Liu G.,Jensen E.R.,Lenoy E.,Schneewind O.
Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections.
Proc. Natl. Acad. Sci. U.S.A.
97
5510-5515
2000
102803
Ton-That H.,Mazmanian S.K.,Alksne L.,Schneewind O.
Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Cysteine 184 and histidine 120 of sortase form a thiolate-imidazolium ion pair for catalysis.
J. Biol. Chem.
277
7447-7452
2002
102804
Perry A.M.,Ton-That H.,Mazmanian S.K.,Schneewind O.
Anchoring of surface proteins to the cell wall of Staphylococcus aureus. III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring.
J. Biol. Chem.
277
16241-16248
2002
102805
Huang X.,Aulabaugh A.,Ding W.,Kapoor B.,Alksne L.,Tabei K.,Ellestad G.
Kinetic mechanism of Staphylococcus aureus sortase SrtA.
Biochemistry
42
11307-11315
2003
102806
Kruger R.G.,Otvos B.,Frankel B.A.,Bentley M.,Dostal P.,McCafferty D.G.
Analysis of the substrate specificity of the Staphylococcus aureus sortase transpeptidase SrtA.
Biochemistry
43
1541-1551
2004
102807
Marraffini L.A.,Ton-That H.,Zong Y.,Narayana S.V.,Schneewind O.
Anchoring of surface proteins to the cell wall of Staphylococcus aureus. A conserved arginine residue is required for efficient catalysis of sortase A.
J. Biol. Chem.
279
37763-37770
2004
102808
Naik M.T.,Suree N.,Ilangovan U.,Liew C.K.,Thieu W.,Campbell D.O.,Clemens J.J.,Jung M.E.,Clubb R.T.
Staphylococcus aureus sortase A transpeptidase. Calcium promotes sorting signal binding by altering the mobility and structure of an active site loop.
J. Biol. Chem.
281
1817-1826
2006
102809
Frankel B.A.,Tong Y.,Bentley M.L.,Fitzgerald M.C.,McCafferty D.G.
Mutational analysis of active site residues in the Staphylococcus aureus transpeptidase SrtA.
Biochemistry
46
7269-7278
2007
102810
Lu C.,Zhu J.,Wang Y.,Umeda A.,Cowmeadow R.B.,Lai E.,Moreno G.N.,Person M.D.,Zhang Z.
Staphylococcus aureus sortase A exists as a dimeric protein in vitro.
Biochemistry
46
9346-9354
2007
102811
Zhu J.,Xiang L.,Jiang F.,Zhang Z.J.
Equilibrium of sortase A dimerization on Staphylococcus aureus cell surface mediates its cell wall sorting activity.
Exp. Biol. Med. (Maywood)
241
90-100
2016
102812
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.
Proc. Natl. Acad. Sci. U.S.A.
98
6056-6061
2001
102813
Zong Y.,Bice T.W.,Ton-That H.,Schneewind O.,Narayana S.V.
Crystal structures of Staphylococcus aureus sortase A and its substrate complex.
J. Biol. Chem.
279
31383-31389
2004
102814
Suree N.,Liew C.K.,Villareal V.A.,Thieu W.,Fadeev E.A.,Clemens J.J.,Jung M.E.,Clubb R.T.
The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized.
J. Biol. Chem.
284
24465-24477
2009
