Annotations for this protein have been verified by the authors of the corresponding papers



DP00208: SortaseFASTA viewXML view

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
         |          |          |          |          |          |
MKKWTNRLMT IAGVVLILVA AYLFAKPHID NYLHDKDKDE KIEQYDKNVK EQASKDKKQQ - 60
AKPQIPKDKS KVAGYIEIPD ADIKEPVYPG PATPEQLNRG VSFAEENESL DDQNISIAGH - 120
TFIDRPNYQF TNLKAAKKGS MVYFKVGNET RKYKMTSIRD VKPTDVGVLD EQKGKDKQLT - 180
LITCDDYNEK TGVWEKRKIF VATEVK



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.

Region 1: 162-174

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.


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:
  1. 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:
  1. 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

  2. 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).




References

  1. 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


If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us.


Disprot-footer
Contact us