| General information | | DisProt: | DP00208 | | Name: | Sortase | | Synonym(s): | Q9S446_STAAU
Sortase A
SrtA
| | First appeared in release: | Release 2.0 (02/14/2005) | | UniProt: | Q9S446 | | UniGene: | | | SwissProt: | Q9S446_STAAU | | TrEMBL: | | | NCBI (GI): | 75421586 | | Source organism: | Staphylococcus aureus | | Sequence length: | 206 | | Percent disordered: | 6% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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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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| Functional narrative |
Sortase A is an important protein in Gram-positive bacteria and play key roles in the pathogenesis of human infections. Located on the cell surface, it facilitates binding by cleaving surface proteins at LPXTG motifs and catalyzes an amide-bond exhange to attach the cleaved protein to a cell-wall crossbridging sequence. Calcium binding near the active site stimulates catalysis. These modifications allow the bacteria to avoid detection by the host's immune system.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Extended | | Name: | disordered loop | | Location: | 162 - 174 | | Length: | 13 | | Region sequence: |
KPTDVGVLDEQKG | | Modification type: | Engineered
| | PDB: | 1IJA:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Substrate/ligand binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (306 K; pH: 6.7; CaCl2 20 mM; DTT 3 mM; H2O 7 %; NaCl 100 mM; NaN3 0.01 %; SrtAN59 protein 2.5 mM; Tris-HCl 50 mM)
| References:
- Ilangovan U, Ton-That H, Iwahara J, Schneewind O, Clubb RT. "Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus." Proc Natl Acad Sci U S A. 2001; 98(11): 6056-61. PubMed: 11371637
- Zong Y, Bice TW, Ton-That H, Schneewind O, Narayana SV. "Crystal structures of Staphylococcus aureus sortase A and its substrate complex." J Biol Chem. 2004; 279(30): 31383-9. PubMed: 15117963
| Comments:The PDB file does not contain the first 59 amino acids of the sequence (Zhong 2004). It was shown that the removal of this N terminal region had no effect on the enzymatic activity of the protein. The disordered region is part of the “catalytic core” of the protein (Ilangovan 2001).
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| References |
- Mazmanian SK, Liu G, Ton-That H, Schneewind O. "Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall." Science. 1999; 285(5428): 760-3. PubMed: 10427003
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